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TitleStructural Analysis of the Glycine Oxidase Homologue CmiS2 Reveals a Unique Substrate Recognition Mechanism for Formation of a beta-Amino Acid Starter Unit in Cremimycin Biosynthesis.
Journal, issue, pagesBiochemistry, Vol. 58, Page 2706-2709, Year 2019
Publish dateJan 4, 2019 (structure data deposition date)
AuthorsKawasaki, D. / Chisuga, T. / Miyanaga, A. / Kudo, F. / Eguchi, T.
External linksBiochemistry / PubMed:31154757
MethodsX-ray diffraction
Resolution2.3 - 2.45 Å
Structure data

PDB-6j38:
Crystal structure of CmiS2
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-6j39:
Crystal structure of CmiS2 with inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HOH:
WATER

ChemComp-B6X:
(3R)-3-[(carboxymethyl)sulfanyl]nonanoic acid

Source
  • streptomyces sp. mj635-86f5 (bacteria)
KeywordsOXIDOREDUCTASE / Flavoenzyme / Polyketide biosynthesis / OXIDOREDUCTASE/INHIBITOR / OXIDOREDUCTASE-INHIBITOR complex

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