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Structure paper

TitleThe dimerization domain in DapE enzymes is required for catalysis.
Journal, issue, pagesPlos One, Vol. 9, Page e93593-e93593, Year 2014
Publish dateSep 12, 2012 (structure data deposition date)
AuthorsNocek, B. / Starus, A. / Makowska-Grzyska, M. / Gutierrez, B. / Sanchez, S. / Jedrzejczak, R. / Mack, J.C. / Olsen, K.W. / Joachimiak, A. / Holz, R.C.
External linksPlos One / PubMed:24806882
MethodsX-ray diffraction
Resolution1.65 - 1.84 Å
Structure data

PDB-4h2k:
Crystal structure of the catalytic domain of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-4onw:
Crystal structure of the catalytic domain of DapE protein from V.cholerea
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4op4:
Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form
Method: X-RAY DIFFRACTION / Resolution: 1.651 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-BU1:
1,4-BUTANEDIOL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACT:
ACETATE ION

Source
  • haemophilus influenzae (bacteria)
  • vibrio cholerae o1 biovar el tor (bacteria)
KeywordsHYDROLASE / DapE / MCSG / PSI-Biology / Structural Genomics / Midwest Center for Structural Genomics / Zinc-dependent hydrolase / M20 / aminopeptidase / CSGID / NIAID / National Institute of Allergy and Infectious Diseases / Center for Structural Genomics of Infectious Diseases / Zn binding

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