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Structure paper

TitleCrystal structure and molecular mechanism of an aspartate/glutamate racemase from Escherichia coli O157
Journal, issue, pagesFebs Lett., Vol. 590, Page 1262-1269, Year 2016
Publish dateJan 22, 2016 (structure data deposition date)
AuthorsLiu, X. / Gao, F. / Ma, Y. / Liu, S. / Cui, Y. / Yuan, Z. / Kang, X.
External linksFebs Lett. / PubMed:27001440
MethodsX-ray diffraction
Resolution1.597 - 1.765 Å
Structure data

PDB-5hqt:
Crystal structure of an aspartate/glutamate racemase from Escherichia coli O157
Method: X-RAY DIFFRACTION / Resolution: 1.598 Å

PDB-5hra:
Crystal structure of an aspartate/glutamate racemase in complex with D-aspartate
Method: X-RAY DIFFRACTION / Resolution: 1.597 Å

PDB-5hrc:
Crystal structure of an aspartate/glutamate racemase in complex with L-aspartate
Method: X-RAY DIFFRACTION / Resolution: 1.765 Å

Chemicals

ChemComp-NHE:
2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-DAS:
D-ASPARTIC ACID

ChemComp-ASP:
ASPARTIC ACID

Source
  • escherichia coli o157:h7 str. ss52 (bacteria)
KeywordsISOMERASE / Aspartate/glutamate racemase / PLP-independent racemase / Racemization mechanism

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