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Crystal structure of LysZ from Thermus thermophilus with ADP
Structural highlights
FunctionLYSZ_THET2 Catalyzes the phosphorylation of LysW-gamma-alpha-aminoadipate. Does not phosphorylate N-acetyl-glutamate.[1] Publication Abstract from PubMedIn the biosynthesis of lysine by Thermus thermophilus, the metabolite alpha-ketoglutarate is converted to the intermediate alpha-aminoadipate (AAA), which is protected by the 54-amino acid acidic protein LysW. In this study, we determined the crystal structure of LysZ from T. thermophilus (TtLysZ), an amino acid kinase that catalyzes the second step in the AAA to lysine conversion, which was in a complex with LysW at a resolution of 1.85 A. A crystal analysis coupled with isothermal titration calorimetry of the TtLysZ mutants for TtLysW revealed tight interactions between LysZ and the globular and C-terminal extension domains of the LysW protein, which were mainly attributed to electrostatic forces. These results provided structural evidence for LysW acting as a protecting molecule for the alpha-amino group of AAA and also as a carrier protein to guarantee better recognition by biosynthetic enzymes for the efficient biosynthesis of lysine. Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ.LysW complex from Thermus thermophilus.,Yoshida A, Tomita T, Fujimura T, Nishiyama C, Kuzuyama T, Nishiyama M J Biol Chem. 2015 Jan 2;290(1):435-47. doi: 10.1074/jbc.M114.595983. Epub 2014, Nov 12. PMID:25392000[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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