5dzt | pdb_00005dzt

Crystal structure of class II lanthipeptide synthetase CylM in complex with AMP

spinqualitylabelsall models 5dzt, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dzt is a 1 chain structure with sequence from Enterococcus faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: AMP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8KUA3_ENTFL Publication Abstract from PubMed The enterococcal cytolysin is a virulence factor consisting of two post-translationally modified peptides that synergistically kill human immune cells. Both peptides are made by CylM, a member of the LanM lanthipeptide synthetases. CylM catalyzes seven dehydrations of Ser and Thr residues and three cyclization reactions during the biosynthesis of the cytolysin large subunit. We present here the 2.2 A resolution structure of CylM, the first structural information on a LanM. Unexpectedly, the structure reveals that the dehydratase domain of CylM resembles the catalytic core of eukaryotic lipid kinases, despite the absence of clear sequence homology. The kinase and phosphate elimination active sites that affect net dehydration are immediately adjacent to each other. Characterization of mutants provided insights into the mechanism of the dehydration process. The structure is also of interest because of the interactions of human homologs of lanthipeptide cyclases with kinases such as mammalian target of rapamycin. The enterococcal cytolysin synthetase has an unanticipated lipid kinase fold.,Dong SH, Tang W, Lukk T, Yu Y, Nair SK, van der Donk WA Elife. 2015 Jul 30;4. doi: 10.7554/eLife.07607. PMID:26226635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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