| Structural highlights
Publication Abstract from PubMed
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 alpha2beta2 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 alpha2beta2-type AK. Moreover, the various inhibitory effectors of PaAK have been identified and a general amino acid effector motif of AK family is described.
Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase.,Li CC, Yang MJ, Liu L, Li T, Peng CT, He LH, Song YJ, Zhu YB, Shen YL, Yang J, Zhao NL, Zhao C, Zhou QX, Li H, Kang M, Tong AP, Tang H, Bao R Biochem J. 2018 Mar 20;475(6):1107-1119. doi: 10.1042/BCJ20170829. PMID:29382741[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li CC, Yang MJ, Liu L, Li T, Peng CT, He LH, Song YJ, Zhu YB, Shen YL, Yang J, Zhao NL, Zhao C, Zhou QX, Li H, Kang M, Tong AP, Tang H, Bao R. Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase. Biochem J. 2018 Mar 20;475(6):1107-1119. doi: 10.1042/BCJ20170829. PMID:29382741 doi:http://dx.doi.org/10.1042/BCJ20170829
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