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3sgl
From Proteopedia
Contents |
The crystal structure of MnmC from Yersinia pestis bound with FAD and SAM
Template:ABSTRACT PUBMED 23617613
Function
[MNMC_YERPE] Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34 (By similarity).
About this Structure
3sgl is a 1 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900. Full crystallographic information is available from OCA.
Reference
- Kim J, Almo SC. Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC. BMC Struct Biol. 2013 Apr 24;13:5. doi: 10.1186/1472-6807-13-5. PMID:23617613 doi:10.1186/1472-6807-13-5
Categories: Almo, S C. | Kim, J. | NYSGRC, New York Structural Genomics Research Consortium. | Fad binding sam binding | Methyltransferase | New york structural genomics research consortium | Nysgrc | Oxidoreductase | Protein structure initiative | Psi-biology | Rossmann fold | Structural genomic | Transferase
