3PS9
Crystal structure of MnmC from E. coli
Summary for 3PS9
| Entry DOI | 10.2210/pdb3ps9/pdb |
| Descriptor | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC, FLAVIN-ADENINE DINUCLEOTIDE, S-ADENOSYLMETHIONINE, ... (5 entities in total) |
| Functional Keywords | rossmann fold, oxidase, methyl transferase, fad, sam binding, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 76564.15 |
| Authors | Kim, J.,Almo, S.C. (deposition date: 2010-12-01, release date: 2010-12-22, Last modification date: 2024-02-21) |
| 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 Cited by 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: 23617613DOI: 10.1186/1472-6807-13-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.54 Å) |
Structure validation
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