6A2F

Crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa

6A2F の概要

• エントリーDOI: 10.2210/pdb6a2f/pdb
• 分子名称: Alanine racemase, biosynthetic, MALONATE ION, D-LYSINE, ... (5 entities in total)
• 機能のキーワード: alanine racemase, alr, pseudomonas aeruginosa, l-alanine, d-alanine, isomerase
• 由来する生物種: Pseudomonas aeruginosa PAO1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77780.46

構造登録者

Dong, H.,Li, S. (登録日: 2018-06-11, 公開日: 2018-08-08, 最終更新日: 2023-11-22)

主引用文献

Dong, H.,Han, Q.,Guo, Y.,Ju, J.,Wang, S.,Yuan, C.,Long, W.,He, X.,Xu, S.,Li, S.
Enzymatic characterization and crystal structure of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1.
Biochem.Biophys.Res.Commun., 503:2319-2325, 2018

PubMed Abstract: Alanine racemase is a pyridoxal-5'-phosphate (PLP)-dependent enzyme that reversibly catalyzes the conversion of l-alanine to d-alanine. d-alanine is an essential constituent in many prokaryotic cell structures. Inhibition of alanine racemase is lethal to prokaryotes, creating an attractive target for designing antibacterial drugs. Here we report the crystal structure of biosynthetic alanine racemase (Alr) from a pathogenic bacteria Pseudomonas aeruginosa PAO1. Structural studies showed that P. aeruginosa Alr (PaAlr) adopts a conserved homodimer structure. A guest substrate d-lysine was observed in the active site and refined to dual-conformation. Two buffer ions, malonate and acetate, were bound in the proximity to d-lysine. Biochemical characterization revealed the optimal reaction conditions for PaAlr.

PubMed: 29964014
DOI: 10.1016/j.bbrc.2018.06.155

実験手法

X-RAY DIFFRACTION (2.5 Å)