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Structure paper

TitleFunctional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli.
Journal, issue, pagesBiochemistry, Vol. 48, Page 7673-7685, Year 2009
Publish dateJan 12, 2009 (structure data deposition date)
AuthorsLee, M.N. / Takawira, D. / Nikolova, A.P. / Ballou, D.P. / Furtado, V.C. / Phung, N.L. / Still, B.R. / Thorstad, M.K. / Tanner, J.J. / Trimmer, E.E.
External linksBiochemistry / PubMed:19610625
MethodsX-ray diffraction
Resolution1.65 - 1.7 Å
Structure data

PDB-3fst:
Crystal Structure of Escherichia coli Methylenetetrahydrofolate Reductase Mutant Phe223Leu at pH 7.4
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3fsu:
Crystal Structure of Escherichia coli Methylenetetrahydrofolate Reductase Double Mutant Phe223LeuGlu28Gln complexed with methyltetrahydrofolate
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

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

ChemComp-MRY:
MESO-ERYTHRITOL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-C2F:
5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID

Source
  • escherichia coli k-12 (bacteria)
KeywordsOXIDOREDUCTASE / TIM BARREL / FLAVIN / REDUCTASE / Amino-acid biosynthesis / FAD / Flavoprotein / Methionine biosynthesis / NAD / NADP / METHYLTETRAHYDROFOLATE

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