NCZS_STRCZ
ID NCZS_STRCZ Reviewed; 147 AA.
AC P0A3R9; P01550;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Neocarzinostatin;
DE Short=NCS;
DE AltName: Full=Mitomalcin;
DE Short=MMC;
DE Flags: Precursor;
GN Name=ncsA;
OS Streptomyces carzinostaticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1897;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15944 / E-793 / F-51;
RX PubMed=8369747; DOI=10.1248/bpb.16.26;
RA Sakata N., Minamitani S., Kanbe T., Hori M., Hamada M., Edo K.;
RT "The amino acid sequence of neocarzinostatin apoprotein deduced from the
RT base sequence of the gene.";
RL Biol. Pharm. Bull. 16:26-28(1993).
RN [2]
RP PROTEIN SEQUENCE OF 35-147.
RX PubMed=2938543; DOI=10.1016/0003-9861(86)90464-9;
RA Kuromizu K., Tsunasawa S., Maeda H., Abe O., Sakiyama F.;
RT "Reexamination of the primary structure of an antitumor protein,
RT neocarzinostatin.";
RL Arch. Biochem. Biophys. 246:199-205(1986).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 35-147.
RX PubMed=6236220; DOI=10.1016/s0021-9258(18)90583-1;
RA Gibson B.W., Herlihy W.C., Samy T.S.A., Hahm K.-S., Maeda H.,
RA Meienhofer J., Biemann K.;
RT "A revised primary structure for neocarzinostatin based on fast atom
RT bombardment and gas chromatographic-mass spectrometry.";
RL J. Biol. Chem. 259:10801-10806(1984).
RN [4]
RP STRUCTURE BY NMR, AND PROTEIN SEQUENCE OF 35-147.
RX PubMed=1831044; DOI=10.1021/bi00245a009;
RA Gao X., Burkhart W.;
RT "Two- and three-dimensional proton NMR studies of apo-neocarzinostatin.";
RL Biochemistry 30:7730-7739(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=8477746; DOI=10.1111/j.1432-1033.1993.tb17814.x;
RA Teplyakov A., Obmolova G., Wilson K., Kuromizu K.;
RT "Crystal structure of apo-neocarzinostatin at 0.15-nm resolution.";
RL Eur. J. Biochem. 213:737-741(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8235619; DOI=10.1126/science.8235619;
RA Kim K.-H., Kwon B.-M., Myers A.G., Rees D.C.;
RT "Crystal structure of neocarzinostatin, an antitumor protein-chromophore
RT complex.";
RL Science 262:1042-1046(1993).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=1533878; DOI=10.1016/0022-2836(92)91030-s;
RA Gao X.;
RT "Three-dimensional solution structure of apo-neocarzinostatin.";
RL J. Mol. Biol. 225:125-135(1992).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=2142075; DOI=10.1111/j.1432-1033.1990.tb15571.x;
RA Adjadj E., Mispelter J., Quiniou E., Dimicoli J.-L., Favaudon V.,
RA Lhoste J.-M.;
RT "Proton NMR studies of apo-neocarzinostatin from Streptomyces
RT carzinostaticus. Sequence-specific assignment and secondary structure.";
RL Eur. J. Biochem. 190:263-271(1990).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=1531194; DOI=10.1111/j.1432-1033.1992.tb16576.x;
RA Adjadj E., Quiniou E., Mispelter J., Favaudon V., Lhoste J.-M.;
RT "Three-dimensional solution structure of apo-neocarzinostatin from
RT Streptomyces carzinostaticus determined by NMR spectroscopy.";
RL Eur. J. Biochem. 203:505-511(1992).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=2147566; DOI=10.1021/bi00488a029;
RA Remerowski M.L., Glaser S.J., Sieker L.C., Samy T.S.A., Drobny G.P.;
RT "Sequential 1H NMR assignments and secondary structure of
RT aponeocarzinostatin in solution.";
RL Biochemistry 29:8401-8409(1990).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=1834636; DOI=10.1093/oxfordjournals.jbchem.a123462;
RA Takashima H., Amiya S., Kobayashi Y.;
RT "Neocarzinostatin: interaction between the antitumor-active chromophore and
RT the carrier protein.";
RL J. Biochem. 109:807-810(1991).
RN [12]
RP DISULFIDE BONDS.
RX PubMed=1832834; DOI=10.1016/0003-9861(91)90081-s;
RA Kuromizu K., Abe O., Maeda H.;
RT "Location of the disulfide bonds in the antitumor protein
RT neocarzinostatin.";
RL Arch. Biochem. Biophys. 286:569-573(1991).
CC -!- FUNCTION: NCS has antibiotic activity (for Gram-positive bacteria) and
CC antitumor activity (for certain mouse tumors). NCS binds non-covalently
CC to a chromophore which is the cytotoxic and mutagenic component of the
CC antibiotic. The chromophore binds to DNA as a weak intercalator and
CC causes single- and double-strand breaks.
CC -!- SIMILARITY: Belongs to the neocarzinostatin family. {ECO:0000305}.
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DR EMBL; D10996; BAA01764.1; -; Genomic_DNA.
DR EMBL; S65575; AAB28103.1; -; Genomic_DNA.
DR PIR; JH0792; ZNSMCC.
DR PDB; 1J5H; NMR; -; A=35-147.
DR PDB; 1J5I; NMR; -; A=35-147.
DR PDB; 1NCO; X-ray; 1.80 A; A/B=35-147.
DR PDB; 1NOA; X-ray; 1.50 A; A=35-147.
DR PDB; 1O5P; NMR; -; A=35-147.
DR PDB; 2CBM; X-ray; 2.03 A; A=35-146.
DR PDB; 2CBO; X-ray; 1.70 A; A=35-147.
DR PDB; 2CBQ; X-ray; 2.60 A; A/B/C/D/E/F=35-147.
DR PDB; 2CBT; X-ray; 2.20 A; A/B=35-146.
DR PDB; 2G0K; NMR; -; A=35-147.
DR PDB; 2G0L; NMR; -; A=35-147.
DR PDBsum; 1J5H; -.
DR PDBsum; 1J5I; -.
DR PDBsum; 1NCO; -.
DR PDBsum; 1NOA; -.
DR PDBsum; 1O5P; -.
DR PDBsum; 2CBM; -.
DR PDBsum; 2CBO; -.
DR PDBsum; 2CBQ; -.
DR PDBsum; 2CBT; -.
DR PDBsum; 2G0K; -.
DR PDBsum; 2G0L; -.
DR AlphaFoldDB; P0A3R9; -.
DR BMRB; P0A3R9; -.
DR SMR; P0A3R9; -.
DR DrugBank; DB08261; 2-hydroxy-7-methoxy-5-methyl-naphthalene-1-carboxylic acid meso-2,5-dihydroxy-cyclopent-3-enyl ester.
DR DrugBank; DB07776; Flavone.
DR DrugBank; DB08619; Testosterone succinate.
DR EvolutionaryTrace; P0A3R9; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR027273; Neocarzinostatin-like.
DR InterPro; IPR002186; Neocarzinostatin_fam.
DR Pfam; PF00960; Neocarzinostat; 1.
DR PRINTS; PR01885; MACROMOMYCIN.
DR SUPFAM; SSF49319; SSF49319; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; DNA-binding; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:1831044,
FT ECO:0000269|PubMed:2938543"
FT CHAIN 35..147
FT /note="Neocarzinostatin"
FT /id="PRO_0000019461"
FT DISULFID 71..81
FT /evidence="ECO:0000269|PubMed:1832834"
FT DISULFID 122..127
FT /evidence="ECO:0000269|PubMed:1832834"
FT CONFLICT 94
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2CBO"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1J5I"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1NOA"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1NOA"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1J5H"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1J5H"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1NOA"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2CBO"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1NOA"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1J5I"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1J5I"
SQ SEQUENCE 147 AA; 14455 MW; C9BE690CC60AC0C6 CRC64;
MVPISIIRNR VAKVAVGSAA VLGLAVGFQT PAVAAAPTAT VTPSSGLSDG TVVKVAGAGL
QAGTAYDVGQ CAWVDTGVLA CNPADFSSVT ADANGSASTS LTVRRSFEGF LFDGTRWGTV
DCTTAACQVG LSDAAGNGPE GVAISFN
