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TitleImplication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes
Journal, issue, pagesTo Be Published
Publish dateJul 30, 2018 (structure data deposition date)
AuthorsBruner, S.D. / Zagulyaeva, A.A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.7 - 1.8 Å
Structure data

PDB-6e8o:
Crystal structure of aryl acid adenylating enzyme FscC from Fuscachelin NRPS in complex with AMP
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-6e97:
Crystal structure of the aryl acid adenylating enzyme FscC from Fuscachelin NRPS in complex with DHB-adenylate
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-J2J:
5'-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine

Source
  • thermobifida fusca (bacteria)
KeywordsLIGASE / siderophore biosynthesis / NRPS / adenylation domain / thiolation state / dihydroxybenzoic acid activating enzyme

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