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TitleEvolution of Enzymatic Activity in the Enolase Superfamily: Structural Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
Journal, issue, pagesBiochemistry, Vol. 43, Page 5716-5727, Year 2004
Publish dateMar 3, 2004 (structure data deposition date)
AuthorsThoden, J.B. / Taylor-Ringia, E.A. / Garrett, J.B. / Gerlt, J.A. / Holden, H.M. / Rayment, I.
External linksBiochemistry / PubMed:15134446
MethodsX-ray diffraction
Resolution1.87 - 2.3 Å
Structure data

PDB-1sja:
X-ray structure of o-Succinylbenzoate Synthase complexed with N-acetylmethionine
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-1sjb:
X-ray structure of o-succinylbenzoate synthase complexed with o-succinylbenzoic acid
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1sjc:
x-ray structure of o-succinylbenzoate synthase complexed with N-succinyl methionine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1sjd:
x-ray structure of o-succinylbenzoate synthase complexed with n-succinyl phenylglycine
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-AME:
N-ACETYLMETHIONINE

ChemComp-HOH:
WATER

ChemComp-OSB:
2-SUCCINYLBENZOATE

ChemComp-SMG:
N-SUCCINYL METHIONINE

ChemComp-NPG:
N-SUCCINYL PHENYLGLYCINE

Source
  • amycolatopsis sp. (bacteria)
KeywordsLYASE / ISOMERASE / racemase

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