CAPSD_BPMS2
ID CAPSD_BPMS2 Reviewed; 130 AA.
AC P03612;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
OS Escherichia phage MS2 (Bacteriophage MS2).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Levivirus.
OX NCBI_TaxID=329852;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=4555447; DOI=10.1038/237082a0;
RA Min Jou W., Haegeman G., Ysebaert M., Fiers W.;
RT "Nucleotide sequence of the gene coding for the bacteriophage MS2 coat
RT protein.";
RL Nature 237:82-88(1972).
RN [2]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=9207028; DOI=10.1093/nar/25.14.2808;
RA Spingola M., Peabody D.S.;
RT "MS2 coat protein mutants which bind Qbeta RNA.";
RL Nucleic Acids Res. 25:2808-2815(1997).
RN [3]
RP MUTAGENESIS OF THR-46; THR-60; GLU-77 AND PRO-79.
RX PubMed=9469846; DOI=10.1093/nar/26.5.1337;
RA Lago H., Fonseca S.A., Murray J.B., Stonehouse N.J., Stockley P.G.;
RT "Dissecting the key recognition features of the MS2 bacteriophage
RT translational repression complex.";
RL Nucleic Acids Res. 26:1337-1344(1998).
RN [4]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=26608810; DOI=10.1016/j.jmb.2015.11.014;
RA Rolfsson O., Middleton S., Manfield I.W., White S.J., Fan B., Vaughan R.,
RA Ranson N.A., Dykeman E., Twarock R., Ford J., Kao C.C., Stockley P.G.;
RT "Direct evidence for packaging signal-mediated assembly of bacteriophage
RT MS2.";
RL J. Mol. Biol. 428:431-448(2016).
RN [5]
RP REVIEW.
RX PubMed=27144089; DOI=10.1080/21597081.2016.1157666;
RA Stockley P.G., White S.J., Dykeman E., Manfield I., Rolfsson O., Patel N.,
RA Bingham R., Barker A., Wroblewski E., Chandler-Bostock R., Weiss E.U.,
RA Ranson N.A., Tuma R., Twarock R.;
RT "Bacteriophage MS2 genomic RNA encodes an assembly instruction manual for
RT its capsid.";
RL Bacteriophage 6:E1157666-E1157666(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=2330049; DOI=10.1038/345036a0;
RA Valegaard K., Liljas L., Fridborg K., Unge T.;
RT "The three-dimensional structure of the bacterial virus MS2.";
RL Nature 345:36-41(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=1772631; DOI=10.1107/s0108768191006821;
RA Valegard K., Liljas L., Fridborg K., Unge T.;
RT "Structure determination of the bacteriophage MS2.";
RL Acta Crystallogr. B 47:949-960(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=8254664; DOI=10.1006/jmbi.1993.1616;
RA Golmohammadi R., Valegaard K., Fridborg K., Liljas L.;
RT "The refined structure of bacteriophage MS2 at 2.8-A resolution.";
RL J. Mol. Biol. 234:620-639(1993).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH RNA, AND FUNCTION.
RX PubMed=7523953; DOI=10.1038/371623a0;
RA Valegaard K., Murray J.B., Sotckley P.G., Stonehouse N.J., Liljas L.;
RT "Crystal structure of an RNA bacteriophage coat protein-operator complex.";
RL Nature 371:623-626(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF TRP-83.
RX PubMed=7788292; DOI=10.1016/s0969-2126(01)00156-3;
RA Ni C.Z., Syed R., Kodandapani R., Wickersham J., Peabody D.S., Ely K.R.;
RT "Crystal structure of the MS2 coat protein dimer: implications for RNA
RT binding and virus assembly.";
RL Structure 3:255-263(1995).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8594200; DOI=10.1006/jmbi.1996.0089;
RA Stonehouse N.J., Valegaard K., Golmohammadi R., van den Worm S., Walton C.,
RA Stockley P.G., Liljas L.;
RT "Crystal structures of MS2 capsids with mutations in the subunit FG loop.";
RL J. Mol. Biol. 256:330-339(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH RNA, FUNCTION, AND
RP RNA-BINDING.
RX PubMed=9245600; DOI=10.1006/jmbi.1997.1144;
RA Valegard K., Murray J.B., Stonehouse N.J., van den Worm S., Stockley P.G.,
RA Liljas L.;
RT "The three-dimensional structures of two complexes between recombinant MS2
RT capsids and RNA operator fragments reveal sequence-specific protein-RNA
RT interactions.";
RL J. Mol. Biol. 270:724-738(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RNA, AND
RP RNA-BINDING.
RX PubMed=9461079; DOI=10.1038/nsb0298-133;
RA Convery M.A., Rowsell S., Stonehouse N.J., Ellington A.D., Hirao I.,
RA Murray J.B., Peabody D.S., Phillips S.E.V., Stockley P.G.;
RT "Crystal structure of an RNA aptamer-protein complex at 2.8-A resolution.";
RL Nat. Struct. Biol. 5:133-139(1998).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RNA.
RX PubMed=9808042; DOI=10.1038/2946;
RA Rowsell S., Stonehouse N.J., Convery M.A., Adams C.J., Ellington A.D.,
RA Hirao I., Peabody D.S., Stockley P.G., Phillips S.E.;
RT "Crystal structures of a series of RNA aptamers complexed to the same
RT protein target.";
RL Nat. Struct. Biol. 5:970-975(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH RNA, MUTAGENESIS OF
RP THR-46 AND THR-60, FUNCTION, AND RNA-BINDING.
RX PubMed=9469847; DOI=10.1093/nar/26.5.1345;
RA van den Worm S.H., Stonehouse N.J., Valegard K., Murray J.B., Walton C.,
RA Fridborg K., Stockley P.G., Liljas L.;
RT "Crystal structures of MS2 coat protein mutants in complex with wild-type
RT RNA operator fragments.";
RL Nucleic Acids Res. 26:1345-1351(1998).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) IN COMPLEX WITH RNA, AND
RP RNA-BINDING.
RX PubMed=9917072; DOI=10.1017/s1355838299981645;
RA Grahn E., Stonehouse N.J., Murray J.B., van den Worm S., Valegard K.,
RA Fridborg K., Stockley P.G., Liljas L.;
RT "Crystallographic studies of RNA hairpins in complexes with recombinant MS2
RT capsids: implications for binding requirements.";
RL RNA 5:131-138(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RNA.
RX PubMed=11095669; DOI=10.1093/nar/28.23.4611;
RA Grahn E., Stonehouse N.J., Adams C.J., Fridborg K., Beigelman L.,
RA Matulic-Adamic J., Warriner S.L., Stockley P.G., Liljas L.;
RT "Deletion of a single hydrogen bonding atom from the MS2 RNA operator leads
RT to dramatic rearrangements at the RNA-coat protein interface.";
RL Nucleic Acids Res. 28:4611-4616(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RNA, AND
RP RNA-BINDING.
RX PubMed=11720290;
RA Grahn E., Moss T., Helgstrand C., Fridborg K., Sundaram M., Tars K.,
RA Lago H., Stonehouse N.J., Davis D.R., Stockley P.G., Liljas L.;
RT "Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-
RT protein complex.";
RL RNA 7:1616-1627(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) IN COMPLEX WITH RNA, AND
RP RNA-BINDING.
RX PubMed=12060685; DOI=10.1093/nar/gkf371;
RA Helgstrand C., Grahn E., Moss T., Stonehouse N.J., Tars K., Stockley P.G.,
RA Liljas L.;
RT "Investigating the structural basis of purine specificity in the structures
RT of MS2 coat protein RNA translational operator hairpins.";
RL Nucleic Acids Res. 30:2678-2685(2002).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE VIRION, FUNCTION, AND SUBUNIT.
RX PubMed=12948491; DOI=10.1016/s0022-2836(03)00846-5;
RA Koning R., van den Worm S., Plaisier J.R., van Duin J., Pieter Abrahams J.,
RA Koerten H.;
RT "Visualization by cryo-electron microscopy of genomic RNA that binds to the
RT protein capsid inside bacteriophage MS2.";
RL J. Mol. Biol. 332:415-422(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH RNA.
RX PubMed=15496523; DOI=10.1261/rna.7710304;
RA Horn W.T., Convery M.A., Stonehouse N.J., Adams C.J., Liljas L.,
RA Phillips S.E., Stockley P.G.;
RT "The crystal structure of a high affinity RNA stem-loop complexed with the
RT bacteriophage MS2 capsid: further challenges in the modeling of ligand-RNA
RT interactions.";
RL RNA 10:1776-1782(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH RNA, AND FUNCTION.
RX PubMed=16531233; DOI=10.1016/j.str.2005.12.006;
RA Horn W.T., Tars K., Grahn E., Helgstrand C., Baron A.J., Lago H.,
RA Adams C.J., Peabody D.S., Phillips S.E., Stonehouse N.J., Liljas L.,
RA Stockley P.G.;
RT "Structural basis of RNA binding discrimination between bacteriophages
RT Qbeta and MS2.";
RL Structure 14:487-495(2006).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS), AND FUNCTION.
RX PubMed=18662904; DOI=10.1110/ps.036905.108;
RA Plevka P., Tars K., Liljas L.;
RT "Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to
RT octahedral particles.";
RL Protein Sci. 17:1731-1739(2008).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (4.70 ANGSTROMS), AND SUBUNIT.
RX PubMed=19521994; DOI=10.1002/pro.184;
RA Plevka P., Tars K., Liljas L.;
RT "Structure and stability of icosahedral particles of a covalent coat
RT protein dimer of bacteriophage MS2.";
RL Protein Sci. 18:1653-1661(2009).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (39.00 ANGSTROMS) IN COMPLEX WITH F-PILUS,
RP AND SUBCELLULAR LOCATION.
RX PubMed=23810697; DOI=10.1016/j.str.2013.05.012;
RA Dent K.C., Thompson R., Barker A.M., Hiscox J.A., Barr J.N., Stockley P.G.,
RA Ranson N.A.;
RT "The asymmetric structure of an icosahedral virus bound to its receptor
RT suggests a mechanism for genome release.";
RL Structure 21:1225-1234(2013).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-130.
RX PubMed=27549001; DOI=10.1021/acs.nanolett.6b02948;
RA Asensio M.A., Morella N.M., Jakobson C.M., Hartman E.C., Glasgow J.E.,
RA Sankaran B., Zwart P.H., Tullman-Ercek D.;
RT "A selection for assembly reveals that a single amino acid mutant of the
RT bacteriophage MS2 coat protein forms a smaller virus-like particle.";
RL Nano Lett. 16:5944-5950(2016).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 26 nm in diameter, and consisting of 89
CC capsid proteins dimers (178 capsid proteins) (PubMed:8254664,
CC PubMed:18662904). Involved in viral genome encapsidation through the
CC interaction between a capsid protein dimer and the multiple packaging
CC signals present in the RNA genome (PubMed:9469847, PubMed:26608810,
CC PubMed:7523953). The capsid contains also 1 copy of the A2 maturation
CC protein (PubMed:8254664). {ECO:0000269|PubMed:12948491,
CC ECO:0000269|PubMed:18662904, ECO:0000269|PubMed:26608810,
CC ECO:0000269|PubMed:7523953, ECO:0000269|PubMed:9469847,
CC ECO:0000305|PubMed:8254664}.
CC -!- FUNCTION: Acts as a translational repressor of viral replicase
CC synthesis late in infection. This latter function is the result of
CC capsid protein interaction with an RNA hairpin which contains the
CC replicase ribosome-binding site. {ECO:0000269|PubMed:16531233,
CC ECO:0000269|PubMed:9207028, ECO:0000269|PubMed:9245600}.
CC -!- SUBUNIT: Homodimer (PubMed:8254664, PubMed:7788292, PubMed:19521994).
CC The capsid proteins form dimers that assemble by group of 5. Twelve
CC such pentamers are linked together with free dimers (PubMed:8254664).
CC The homodimers binds to the viral RNA via an operator hairpin, but also
CC to many other RNA sequences in the viral genome; this interaction
CC probably shifts the virus from the replicative to the assembly phase
CC and ensures specific encapsidation of the viral genome
CC (PubMed:12948491). {ECO:0000269|PubMed:19521994,
CC ECO:0000269|PubMed:7788292, ECO:0000269|PubMed:8254664,
CC ECO:0000305|PubMed:12948491}.
CC -!- INTERACTION:
CC P03612; P03612: -; NbExp=2; IntAct=EBI-781118, EBI-781118;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8254664}. Note=The
CC shell is composed of 178 copies of the capsid protein and 1 copy of the
CC maturation protein. {ECO:0000269|PubMed:23810697,
CC ECO:0000305|PubMed:8254664}.
CC -!- SIMILARITY: Belongs to the Levivirus capsid protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1e7x";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure assembled from a chemically modified RNA genome hairpin
CC variant;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1dzs";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure assembled from a modified RNA genome hairpin variant G7;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1gkv";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure assembled from modified RNA genome hairpin variant G10;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1gkw";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure assembled from modified RNA genome hairpin variant C10;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1kuo";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant E77D;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1mst";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant T60S;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1aq3";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant T46A;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1aq4";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant T46A;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1mva";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant T60S;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1mvb";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure of mutant P79N;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1bms";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with 8 nt RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1zdj";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with 19 nt RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1zdh";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with 19 nt RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1zdi";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with 23 nt RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1zdk";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=2ms2";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with a aptamer RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=6msf";
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure associated with a F5 aptamer RNA;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=1u1y";
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DR EMBL; V00642; CAA23989.1; -; mRNA.
DR PIR; B04222; VCBPM2.
DR RefSeq; NP_040648.1; NC_001417.2.
DR PDB; 1AQ3; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 1AQ4; X-ray; 3.00 A; A/B/C=2-130.
DR PDB; 1BMS; X-ray; 2.70 A; A/B/C=2-130.
DR PDB; 1MSC; X-ray; 2.00 A; A=2-130.
DR PDB; 1MST; X-ray; 2.60 A; A/B/C=2-130.
DR PDB; 1MVA; X-ray; 3.00 A; A/B/C=2-130.
DR PDB; 1MVB; X-ray; 3.00 A; A/B/C=2-130.
DR PDB; 1U1Y; X-ray; 2.85 A; A/B/C=2-130.
DR PDB; 1ZDH; X-ray; 2.70 A; A/B/C=2-130.
DR PDB; 1ZDI; X-ray; 2.70 A; A/B/C=2-130.
DR PDB; 1ZDJ; X-ray; 2.90 A; A/B/C=2-130.
DR PDB; 1ZDK; X-ray; 2.86 A; A/B/C=2-130.
DR PDB; 1ZSE; X-ray; 3.00 A; A/B/C=2-130.
DR PDB; 2B2D; X-ray; 2.90 A; A/B/C=2-130.
DR PDB; 2B2E; X-ray; 3.15 A; A/B/C=2-130.
DR PDB; 2B2G; X-ray; 3.02 A; A/B/C=2-130.
DR PDB; 2BNY; X-ray; 3.00 A; A/B/C=2-130.
DR PDB; 2BQ5; X-ray; 2.91 A; A/B/C=2-130.
DR PDB; 2BS0; X-ray; 2.45 A; A/B/C=2-130.
DR PDB; 2BS1; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 2BU1; X-ray; 2.20 A; A/B/C=2-130.
DR PDB; 2C4Q; X-ray; 2.38 A; A/B/C=2-130.
DR PDB; 2C4Y; X-ray; 2.68 A; A/B/C=2-130.
DR PDB; 2C4Z; X-ray; 2.60 A; A/B/C=2-130.
DR PDB; 2C50; X-ray; 2.65 A; A/B/C=2-130.
DR PDB; 2C51; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 2IZ8; X-ray; 3.30 A; A/B/C=2-130.
DR PDB; 2IZ9; X-ray; 2.85 A; A/B/C=2-130.
DR PDB; 2IZM; X-ray; 2.70 A; A/B/C=2-130.
DR PDB; 2IZN; X-ray; 2.56 A; A/B/C=2-130.
DR PDB; 2MS2; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 2VTU; X-ray; 3.50 A; J/L=2-130.
DR PDB; 2WBH; X-ray; 4.70 A; A/B/C=2-130.
DR PDB; 4BP7; EM; 39.00 A; A0/A1/A2/A3/A4/A5/A6/A7/A8/A9/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/Aa/Ab/Ac/Ad/Ae/Af/Ag/Ah/Ai/Aj/Ak/Al/Am/An/Ao/Ap/Aq/Ar/As/At/Au/Av/Aw/Ax/B0/B1/B2/B3/B4/B5/B6/B7/B8/B9/BA=2-130.
DR PDB; 4ZOR; X-ray; 2.20 A; A/B/C/D/E=2-130.
DR PDB; 5MSF; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 5TC1; EM; 3.60 A; A/B/C/D/E/F/G/H=1-130.
DR PDB; 6MSF; X-ray; 2.80 A; A/B/C=2-130.
DR PDB; 6RRS; EM; 3.90 A; A/B/C=1-130.
DR PDB; 6RRT; EM; 6.00 A; A/B/C/D=1-130.
DR PDB; 7MSF; X-ray; 2.80 A; A/B/C=2-130.
DR PDBsum; 1AQ3; -.
DR PDBsum; 1AQ4; -.
DR PDBsum; 1BMS; -.
DR PDBsum; 1MSC; -.
DR PDBsum; 1MST; -.
DR PDBsum; 1MVA; -.
DR PDBsum; 1MVB; -.
DR PDBsum; 1U1Y; -.
DR PDBsum; 1ZDH; -.
DR PDBsum; 1ZDI; -.
DR PDBsum; 1ZDJ; -.
DR PDBsum; 1ZDK; -.
DR PDBsum; 1ZSE; -.
DR PDBsum; 2B2D; -.
DR PDBsum; 2B2E; -.
DR PDBsum; 2B2G; -.
DR PDBsum; 2BNY; -.
DR PDBsum; 2BQ5; -.
DR PDBsum; 2BS0; -.
DR PDBsum; 2BS1; -.
DR PDBsum; 2BU1; -.
DR PDBsum; 2C4Q; -.
DR PDBsum; 2C4Y; -.
DR PDBsum; 2C4Z; -.
DR PDBsum; 2C50; -.
DR PDBsum; 2C51; -.
DR PDBsum; 2IZ8; -.
DR PDBsum; 2IZ9; -.
DR PDBsum; 2IZM; -.
DR PDBsum; 2IZN; -.
DR PDBsum; 2MS2; -.
DR PDBsum; 2VTU; -.
DR PDBsum; 2WBH; -.
DR PDBsum; 4BP7; -.
DR PDBsum; 4ZOR; -.
DR PDBsum; 5MSF; -.
DR PDBsum; 5TC1; -.
DR PDBsum; 6MSF; -.
DR PDBsum; 6RRS; -.
DR PDBsum; 6RRT; -.
DR PDBsum; 7MSF; -.
DR SMR; P03612; -.
DR DIP; DIP-37669N; -.
DR EvolutionaryTrace; P03612; -.
DR Proteomes; UP000002127; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:1904972; P:negative regulation of viral translation; IDA:CACAO.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.380.10; -; 1.
DR InterPro; IPR002703; Levivir_coat.
DR InterPro; IPR015954; Phage_RNA-type_capsid.
DR Pfam; PF01819; Levi_coat; 1.
DR SUPFAM; SSF55405; SSF55405; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; RNA-binding;
KW T=3 icosahedral capsid protein; Translation regulation; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250|UniProtKB:P69171"
FT CHAIN 2..130
FT /note="Capsid protein"
FT /id="PRO_0000164843"
FT REGION 32..105
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000269|PubMed:26608810"
FT MUTAGEN 46
FT /note="T->A: Loss of repression of replicase translation.
FT 80% loss of binding to the operator RNA in vivo."
FT /evidence="ECO:0000269|PubMed:9469846,
FT ECO:0000269|PubMed:9469847"
FT MUTAGEN 60
FT /note="T->S: Loss of repression of replicase. 20% loss of
FT binding to the operator RNA in vivo."
FT /evidence="ECO:0000269|PubMed:9469846,
FT ECO:0000269|PubMed:9469847"
FT MUTAGEN 77
FT /note="E->A: No effect on the organization of the T=3
FT capsid, but with a loss of thermal stability. No effect on
FT infectivity."
FT /evidence="ECO:0000269|PubMed:9469846"
FT MUTAGEN 79
FT /note="P->A: No effect on the organization of the T=3
FT capsid, but with a loss of thermal stability. Complete loss
FT of infectivity."
FT /evidence="ECO:0000269|PubMed:9469846"
FT MUTAGEN 83
FT /note="W->R: Complete loss of viral assembly."
FT /evidence="ECO:0000269|PubMed:7788292"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:4ZOR"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2VTU"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2VTU"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:1MSC"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:1MSC"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2VTU"
SQ SEQUENCE 130 AA; 13860 MW; ABCDD9FD8B188C6A CRC64;
MASNFTQFVL VDNGGTGDVT VAPSNFANGV AEWISSNSRS QAYKVTCSVR QSSAQNRKYT
IKVEVPKVAT QTVGGVELPV AAWRSYLNME LTIPIFATNS DCELIVKAMQ GLLKDGNPIP
SAIAANSGIY
