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TitleEvolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed by o-Succinylbenzoate Synthase from Escherichia coli
Journal, issue, pagesBiochemistry, Vol. 42, Page 14427-14433, Year 2003
Publish dateOct 17, 2003 (structure data deposition date)
AuthorsKlenchin, V.A. / Taylor Ringia, E.A. / Gerlt, J.A. / Rayment, I.
External linksBiochemistry / PubMed:14661953
MethodsX-ray diffraction
Resolution1.62 Å
Structure data

PDB-1r6w:
Crystal structure of the K133R mutant of o-Succinylbenzoate synthase (OSBS) from Escherichia coli. Complex with SHCHC
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-164:
2-(3-CARBOXYPROPIONYL)-6-HYDROXY-CYCLOHEXA-2,4-DIENE CARBOXYLIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsLYASE / Enolase superfamily; TIM barrel; capping alpha+beta domain

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