3 years ago

Mechanistic insight into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase.

Hong Tang, Chang-Cheng Li, Hong Li, Ying-Jie Song, Ai-Ping Tong, Mei-Jia Yang, Tao Li, Chang Zhao, Ya-Lin Shen, Li Liu, Qiao-Xia Zhou, Cui-Ting Peng, Jing Yang, Li-Hui He, Yi-Bo Zhu, Rui Bao, Ning-Lin Zhao, Mei Kang
In plants and microorganisms, aspartate kinase (AK) catalyzes an initial commitment step of the aspartate family amino acids biosynthesis. Due to various structural organization, 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 clarify 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.

Publisher URL: http://doi.org/10.1042/BCJ20170829

DOI: 10.1042/BCJ20170829

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