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TitleAclacinomycin 10-Hydroxylase Is a Novel Substrate-assisted Hydroxylase Requiring S-Adenosyl-L-methionine as Cofactor
Journal, issue, pagesJ. Biol. Chem., Vol. 280, Page 3636-3644, Year 2005
Publish dateSep 8, 2004 (structure data deposition date)
AuthorsJansson, A. / Koskiniemi, H. / Erola, A. / Wang, J. / Schneider, G. / Niemi, J.
External linksJ. Biol. Chem. / PubMed:15548527
MethodsX-ray diffraction
Resolution2.3 - 2.7 Å
Structure data

PDB-1xds:
Crystal structure of Aclacinomycin-10-hydroxylase (RdmB) in complex with S-adenosyl-L-methionine (SAM) and 11-deoxy-beta-rhodomycin (DbrA)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1xdu:
Crystal structure of Aclacinomycin-10-hydroxylase (RdmB) in complex with Sinefungin (SFG)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-DRA:
11-DEOXY-BETA-RHODOMYCIN

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-SFG:
SINEFUNGIN

Source
  • streptomyces purpurascens (bacteria)
KeywordsTRANSFERASE / Anthracycline; hydroxylase; S-adenosyl-L-methionine; streptomyces; polyketide antibiotics; divergent evolution / Structural Proteomics in Europe / SPINE / Structural Genomics / Anthracycline; hydroxylase; S-adenosyl-L-methionine analogue; sinefungin; streptomyces; polyketide antibiotics; divergent evolution

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