3PS9

Crystal structure of MnmC from E. coli

3PS9 の概要

• エントリーDOI: 10.2210/pdb3ps9/pdb
• 分子名称: tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein mnmC, FLAVIN-ADENINE DINUCLEOTIDE, S-ADENOSYLMETHIONINE, ... (5 entities in total)
• 機能のキーワード: rossmann fold, oxidase, methyl transferase, fad, sam binding, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76564.15

構造登録者

Kim, J.,Almo, S.C. (登録日: 2010-12-01, 公開日: 2010-12-22, 最終更新日: 2024-02-21)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.54 Å)