3CES

Crystal Structure of E.coli MnmG (GidA), a Highly-Conserved tRNA Modifying Enzyme

3CES の概要

• エントリーDOI: 10.2210/pdb3ces/pdb
• 分子名称: tRNA uridine 5-carboxymethylaminomethyl modification enzyme gidA (2 entities in total)
• 機能のキーワード: trna modification, fad binding domain, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, rna binding protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm : P0A6U3
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 288203.06

構造登録者

Shi, R.,Matte, A.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (登録日: 2008-02-29, 公開日: 2009-03-03, 最終更新日: 2024-02-21)

主引用文献

Shi, R.,Villarroya, M.,Ruiz-Partida, R.,Li, Y.,Proteau, A.,Prado, S.,Moukadiri, I.,Benitez-Paez, A.,Lomas, R.,Wagner, J.,Matte, A.,Velazquez-Campoy, A.,Armengod, M.E.,Cygler, M.
Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
J.Bacteriol., 191:7614-7619, 2009

PubMed Abstract: The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.

PubMed: 19801413
DOI: 10.1128/JB.00650-09

実験手法

X-RAY DIFFRACTION (2.412 Å)