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TitleStructure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
Journal, issue, pagesJ. Bacteriol., Vol. 191, Page 7614-7619, Year 2009
Publish dateFeb 29, 2008 (structure data deposition date)
AuthorsShi, R. / Villarroya, M. / Ruiz-Partida, R. / Li, Y. / Proteau, A. / Prado, S. / Moukadiri, I. / Benitez-Paez, A. / Lomas, R. / Wagner, J. ...Shi, R. / Villarroya, M. / Ruiz-Partida, R. / Li, Y. / Proteau, A. / Prado, S. / Moukadiri, I. / Benitez-Paez, A. / Lomas, R. / Wagner, J. / Matte, A. / Velazquez-Campoy, A. / Armengod, M.E. / Cygler, M.
External linksJ. Bacteriol. / PubMed:19801413
MethodsX-ray diffraction
Resolution2.412 - 3.49 Å
Structure data

PDB-3ces:
Crystal Structure of E.coli MnmG (GidA), a Highly-Conserved tRNA Modifying Enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.412 Å

PDB-3g05:
Crystal structure of N-terminal domain (2-550) of E.coli MnmG
Method: X-RAY DIFFRACTION / Resolution: 3.49 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli (E. coli)
  • escherichia coli o157:h7 edl933 (bacteria)
KeywordsRNA BINDING PROTEIN / tRNA modification / FAD binding domain / Structural Genomics / Montreal-Kingston Bacterial Structural Genomics Initiative / BSGI / tRNA-modification enzyme / FAD / Flavoprotein / NAD / tRNA processing

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