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Structure paper

TitleCrystal structure of the thioesterification conformation of Bacillus subtilis o-succinylbenzoyl-CoA synthetase reveals a distinct substrate-binding mode
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 12296-12310, Year 2017
Publish dateMar 2, 2017 (structure data deposition date)
AuthorsChen, Y. / Li, T.L. / Lin, X. / Li, X. / Li, X.D. / Guo, Z.
External linksJ. Biol. Chem. / PubMed:28559280
MethodsX-ray diffraction
Resolution1.763 - 1.9 Å
Structure data

PDB-5x8f:
Ternary complex structure of a double mutant I454RA456K of o-Succinylbenzoate CoA Synthetase (MenE) from Bacillus Subtilis bound with AMP and its product analogue OSB-NCoA at 1.76 angstrom
Method: X-RAY DIFFRACTION / Resolution: 1.763 Å

PDB-5x8g:
Binary complex structure of a double mutant I454RA456K of o-Succinylbenzoate CoA Synthetase (MenE) from Bacillus Subtilis bound with its product analogue OSB-NCoA at 1.90 angstrom
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-S0N:
o-succinylbenzoyl-N-coenzyme A

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-MG:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
KeywordsLIGASE / Adenylate-forming Enzyme / acyl-CoA synthetase / thioester conformation / CoA / pantetheine tunnel / ADP binding subsite / domain alternation / large conformational change / inter-domain linker

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