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1MDX

Crystal structure of ArnB transferase with pyridoxal 5' phosphate

1MDX の概要
エントリーDOI10.2210/pdb1mdx/pdb
関連するPDBエントリー1MDO 1MDZ
分子名称UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase, 2-OXOGLUTARIC ACID, GLYCEROL, ... (4 entities in total)
機能のキーワードtype 1 aminotransferase fold, transferase
由来する生物種Salmonella enterica subsp. enterica serovar Typhimurium
タンパク質・核酸の鎖数1
化学式量合計43390.19
構造登録者
主引用文献Noland, B.W.,Newman, J.M.,Hendle, J.,Badger, J.,Christopher, J.A.,Tresser, J.,Buchanan, M.D.,Wright, T.,Rutter, M.E.,Sanderson, W.E.,Muller-Dieckmann, H.-J.,Gajiwala, K.,Buchanan, S.G.
Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: A 4-amino-4-deoxy-L-arabinose lipopolysaccharide modifying enzyme
Structure, 10:1569-1580, 2002
Cited by
PubMed Abstract: Lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system. ArnB catalysis of amino group transfer from glutamic acid to the 4"-position of a UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway. Structural and functional studies of the ArnB aminotransferase were undertaken by combining X-ray crystallography with biochemical analyses. High-resolution crystal structures were solved for two native forms and one covalently inhibited form of S. typhimurium ArnB. These structures permitted identification of key residues involved in substrate binding and catalysis, including a rarely observed nonprolyl cis peptide bond in the active site.
PubMed: 12429098
DOI: 10.1016/S0969-2126(02)00879-1
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.96 Å)
構造検証レポート
Validation report summary of 1mdx
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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