5xoy

Crystal structure of LysK from Thermus thermophilus in complex with Lysine

spinqualitylabelsall models 5xoy, resolution 2.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xoy is a 2 chain structure. This structure supersedes the now removed PDB entry 3x3e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LYS, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LYSK_THET2] Catalyzes the deacetylation of N(2)-acetyllysine. Mainly involved in lysine biosynthesis, but can also catalyze the deacetylation of N(2)-acetylornithine, which means that it could be involved in arginine biosynthesis.[HAMAP-Rule:MF_01120] Publication Abstract from PubMed LysK is an M20 peptidase family enzyme that hydrolyzes the isopeptide bond between the carrier protein LysW and lysine in order to release lysine, which is the last step of lysine biosynthesis in Thermus thermophilus. In the present study, we determined the crystal structure of LysK in complex with lysine at a resolution of 2.4 A. The alpha-amino group of the bound lysine was oriented toward the catalytic center, which was composed of the residues coordinating divalent metal ions for the hydrolysis of the isopeptide bond. An 11 A-long path was observed from the active site binding lysine to the protein surface, which may be responsible for recognizing the C-terminal extension domain of LysW with the conserved EDWGE sequence. A positively-charged surface region was detected around the exit of the path, similar to other lysine biosynthetic enzymes using LysW as the carrier protein. Mutational studies of the surface residues provided a plausible model for the electrostatic interaction with LysW. Crystal structure of LysK, an enzyme catalyzing the last step of lysine biosynthesis in Thermus thermophilus, in complex with lysine: Insight into the mechanism for recognition of the amino-group carrier protein, LysW.,Fujita S, Cho SH, Yoshida A, Hasebe F, Tomita T, Kuzuyama T, Nishiyama M Biochem Biophys Res Commun. 2017 Sep 16;491(2):409-415. doi:, 10.1016/j.bbrc.2017.07.088. Epub 2017 Jul 15. PMID:28720495 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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