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Structure paper

TitleStructural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.
Journal, issue, pagesBmc Struct. Biol., Vol. 13, Page 5-5, Year 2013
Publish dateDec 1, 2010 (structure data deposition date)
AuthorsKim, J. / Almo, S.C.
External linksBmc Struct. Biol. / PubMed:23617613
MethodsX-ray diffraction
Resolution2.31 - 2.7 Å
Structure data

PDB-3ps9:
Crystal structure of MnmC from E. coli
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

PDB-3pvc:
Crystal structure of apo MnmC from Yersinia Pestis
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-3sgl:
The crystal structure of MnmC from Yersinia pestis bound with FAD and SAM
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

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

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
  • yersinia pestis (bacteria)
KeywordsTRANSFERASE / Rossmann Fold / oxidase / methyl transferase / FAD / SAM binding / OXIDOREDUCTASE / Structural Genomics / PSI-BIOLOGY / Protein Structure Initiative / oxidation / methylation / SAM / New York Structural Genomics Research Consortium / NYSGRC / methyltransferase / FAD binding SAM binding

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