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TitleConserved residue His-257 ofVibrio choleraeflavin transferase ApbE plays a critical role in substrate binding and catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 13800-13810, Year 2019
Publish dateFeb 8, 2019 (structure data deposition date)
AuthorsFang, X. / Osipiuk, J. / Chakravarthy, S. / Yuan, M. / Menzer, W.M. / Nissen, D. / Liang, P. / Raba, D.A. / Tuz, K. / Howard, A.J. ...Fang, X. / Osipiuk, J. / Chakravarthy, S. / Yuan, M. / Menzer, W.M. / Nissen, D. / Liang, P. / Raba, D.A. / Tuz, K. / Howard, A.J. / Joachimiak, A. / Minh, D.D.L. / Juarez, O.
External linksJ. Biol. Chem. / PubMed:31350338
MethodsX-ray diffraction
Resolution1.61 - 1.92 Å
Structure data

PDB-6nxi:
Flavin Transferase ApbE from Vibrio cholerae
Method: X-RAY DIFFRACTION / Resolution: 1.61 Å

PDB-6nxj:
Flavin Transferase ApbE from Vibrio cholerae, H257G mutant
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-MG:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • vibrio cholerae (bacteria)
KeywordsTRANSFERASE / ApbE / Flavin Transferase / FAD / structural genomics / Center for Structural Genomics of Infectious Diseases / CSGID

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