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- Title
Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase.
- Authors
Chang-Cheng Li; Mei-Jia Yang; Li Liu; Tao Li; Cui-Ting Peng; Li-Hui He; Ying-Jie Song; Yi-Bo Zhu; Ya-Lin Shen; Jing Yang; Ning-Lin Zhao; Chang Zhao; Qiao-Xia Zhou; Hong Li; Mei Kang; Ai-Ping Tong; Hong Tang; Rui Bao
- 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 Pseudomonas aeruginosa (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.
- Subjects
PSEUDOMONAS aeruginosa; PLANT enzymes; ALLOSTERIC regulation; ASPARTOKINASE; AMINO acid synthesis; MOLECULAR conformation
- Publication
Biochemical Journal, 2018, Vol 475, Issue 6, p1107
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BCJ20170829