5YEI

Mechanistic insight into the regulation of Pseudomonas aeruginosa aspartate kinase

Summary for 5YEI

• Entry DOI: 10.2210/pdb5yei/pdb
• Descriptor: Aspartokinase, THREONINE, LYSINE, ... (6 entities in total)
• Functional Keywords: pseudomonas aeruginosa, aspartate kinase, transferase
• Biological source: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); More
• Total number of polymer chains: 8
• Total formula weight: 250569.45

Authors

Li, C.,Yang, M.,Liu, L.,Peng, C.,Li, T.,He, L.,Song, Y.,Zhu, Y.,Bao, R. (deposition date: 2017-09-17, release date: 2018-08-29, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.301 Å)