3PVC

Crystal structure of apo MnmC from Yersinia Pestis

Summary for 3PVC

• Entry DOI: 10.2210/pdb3pvc/pdb
• Related: 3PS9
• Descriptor: tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC, FLAVIN-ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, psi-biology, protein structure initiative, rossmann fold, oxidation, methylation, fad, sam, oxidoreductase, transferase, new york structural genomics research consortium, nysgrc
• Biological source: Yersinia pestis
• Cellular location: Cytoplasm (Potential): Q8ZD36
• Total number of polymer chains: 1
• Total formula weight: 78185.31

Authors

Kim, J.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC) (deposition date: 2010-12-06, release date: 2011-04-13, Last modification date: 2013-12-25)

Primary citation

Kim, J.,Almo, S.C.
Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC.
Bmc Struct.Biol., 13:5-5, 2013

PubMed Abstract: Methylaminomethyl modification of uridine or 2-thiouridine (mnm5U34 or mnm5s2U34) at the wobble position of tRNAs specific for glutamate, lysine and arginine are observed in Escherichia coli and allow for specific recognition of codons ending in A or G. In the biosynthetic pathway responsible for this post-transcriptional modification, the bifunctional enzyme MnmC catalyzes the conversion of its hypermodified substrate carboxymethylaminomethyl uridine (cmnm5U34) to mnm5U34. MnmC catalyzes the flavin adenine dinucleotide (FAD)-dependent oxidative cleavage of carboxymethyl group from cmnm5U34 via an imine intermediate to generate aminomethyl uridine (nm5U34), which is subsequently methylated by S-adenosyl-L-methionine (SAM) to yield methylaminomethyl uridine (mnm5U34).

PubMed: 23617613
DOI: 10.1186/1472-6807-13-5

Experimental method

X-RAY DIFFRACTION (2.31 Å)