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Structure paper

TitleStructural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 6609-6618, Year 2007
Publish dateJan 9, 2007 (structure data deposition date)
AuthorsDoukov, T.I. / Hemmi, H. / Drennan, C.L. / Ragsdale, S.W.
External linksJ. Biol. Chem. / PubMed:17172470
MethodsX-ray diffraction
Resolution2.2 - 2.3 Å
Structure data

PDB-2e7f:
5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 Angsrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2ogy:
Asn199Ala Mutant of the 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.3 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-CA:
Unknown entry

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

ChemComp-HOH:
WATER

Source
  • moorella thermoacetica (bacteria)
KeywordsTRANSFERASE / Methyltetrahydrofolate-protein complex / corrionoid / vitamin B12 / TIM Barrel

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