5YKR

Crystal structure of a glutamate-1-semialdehyde-aminomutase from Pseudomonas aeruginosa PAO1

5YKR の概要

• エントリーDOI: 10.2210/pdb5ykr/pdb
• 分子名称: Probable aminotransferase (2 entities in total)
• 機能のキーワード: glutamate-1-semialdehyde-aminomutase, c5 pathway, transferase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102630.23

構造登録者

Li, S.,Zhang, Q.,Bartlam, M. (登録日: 2017-10-16, 公開日: 2018-09-26, 最終更新日: 2023-11-22)

主引用文献

Li, S.,Lou, X.,Xu, Y.,Teng, X.,Che, S.,Liu, R.,Bartlam, M.
Crystal structure of a glutamate-1-semialdehyde-aminomutase from Pseudomonas aeruginosa PAO1.
Biochem. Biophys. Res. Commun., 500:804-809, 2018

PubMed Abstract: The C5 pathway in bacteria is responsible for the synthesis of 5-aminolevulinic acid, which forms the core skeleton of cofactors required for metabolism. One of the key actors in this pathway is a pyridoxamine-5'-phosphate (PMP)/pyridoxal-5'-phosphate (PLP) dependent enzyme called glutamate-1-semialdehyde aminomutase (GSAM). In this study, we crystallized the expression product of the uncharacterized pa4088 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1. The resulting high-resolution structure confirms it to be a member of the GSAM family. Continuous electron density indicates the presence of a PLP cofactor with a Schiff base linkage between the PLP cofactor and the ε-amino group of Lys286. A crystal structure of a K286A mutant in complex with PMP is also reported. As GSAM enzymes are not present in mammalian cells, this work provides a starting point for the investigation of GSAM as a target for drug development against P. aeruginosa infection.

PubMed: 29684343
DOI: 10.1016/j.bbrc.2018.04.163

実験手法

X-RAY DIFFRACTION (1.44 Å)