7jvf | pdb_00007jvf

Solution NMR structure of Prochlorosin 2.10 produced by Prochlorococcus MIT 9313

spinqualitylabelsall models 7jvf, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7jvf is a 1 chain structure with sequence from Promm. This structure supersedes the now removed PDB entry 6viq. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: DAL, DBB, DBU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Lanthipeptides are characterized by thioether crosslinks formed by post-translational modifications. The cyclization process that favors a single ring pattern over many other possible ring patterns has been the topic of much speculation. Recent studies suggest that for some systems the cyclization pattern and stereochemistry is determined not by the enzyme, but by the sequence of the precursor peptide. However, the factors that govern the outcome of the cyclization process are not understood. This study presents the three-dimensional structures of seven lanthipeptides determined by nuclear magnetic resonance spectroscopy, including five prochlorosins and the two peptides that make up cytolysin, a virulence factor produced by Enterococcus faecalis that is directly linked to human disease. These peptides were chosen because their substrate sequence determines either the ring pattern (prochlorosins) or the stereochemistry of cyclization (cytolysins). We present the structures of prochlorosins 1.1, 2.1, 2.8, 2.10 and 2.11, the first three-dimensional structures of prochlorosins. Our findings provide insights into the molecular determinants of cyclization as well as why some prochlorosins may be better starting points for library generation than others. The structures of the large and small subunits of the enterococcal cytolysin show that these peptides have long helical stretches, a rare observation for lanthipeptides characterized to date. These helices may explain their pore forming activity and suggest that the small subunit may recognize a molecular target followed by recruitment of the large subunit to span the membrane. Structural determinants of macrocyclization in substrate-controlled lanthipeptide biosynthetic pathways.,Bobeica SC, Zhu L, Acedo JZ, Tang W, van der Donk WA Chem Sci. 2020 Jun 25;11(47):12854-12870. doi: 10.1039/d0sc01651a. PMID:34094481 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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