5YEI

Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase

5YEI の概要

• エントリーDOI: 10.2210/pdb5yei/pdb
• 分子名称: Aspartokinase, THREONINE, LYSINE, ... (6 entities in total)
• 機能のキーワード: pseudomonas aeruginosa, aspartate kinase, 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); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 250569.45

構造登録者

Li, C.,Yang, M.,Liu, L.,Peng, C.,Li, T.,He, L.,Song, Y.,Zhu, Y.,Bao, R. (登録日: 2017-09-17, 公開日: 2018-08-29, 最終更新日: 2023-11-22)

主引用文献

Li, C.,Yang, M.,Liu, L.,Li, T.,Peng, C.,He, L.,Song, Y.,Zhu, Y.,Shen, Y.,Yang, J.,Zhao, N.,Zhao, C.,Zhou, Q.,Li, H.,Kang, M.,Tong, A.,Tang, H.,Bao, R.
Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase.
Biochem.J., 475:1107-1119, 2018

PubMed Abstract: In plants and microorganisms, aspartate kinase (AK) catalyzes an initial commitment step of the aspartate family amino acid biosynthesis. Owing to various structural organizations, AKs from different species show tremendous diversity and complex allosteric controls. We report the crystal structure of AK from (PaAK), a typical α2β2 hetero-tetrameric enzyme, in complex with inhibitory effectors. Distinctive features of PaAK are revealed by structural and biochemical analyses. Essentially, the open conformation of Lys-/Thr-bound PaAK structure clarifies the inhibitory mechanism of α2β2-type AK. Moreover, the various inhibitory effectors of PaAK have been identified and a general amino acid effector motif of AK family is described.

PubMed: 29382741
DOI: 10.1042/BCJ20170829

実験手法

X-RAY DIFFRACTION (2.301 Å)