6m7y | pdb_00006m7y

Dehydratase, NisB, bound to a non-eliminable substrate analog

spinqualitylabelsall models 6m7y, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6m7y is a 4 chain structure with sequence from "lactococcus_lactis_subsp._diacitilactis_(sic)"_(garvie_and_farrow_1982)_schleifer_et_al._1986 "lactococcus lactis subsp. diacitilactis (sic)" (garvie and farrow 1982) schleifer et al. 1986. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: J9A, MSE Gene: nisB ("Lactococcus lactis subsp. diacitilactis (sic)" (Garvie and Farrow 1982) Schleifer et al. 1986) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NISB_LACLL] Involved in the post-translational modification of the lantibiotic nisin. [Q7BB86_9LACT] Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.[RuleBase:RU362078] Publication Abstract from PubMed The peptide natural product nisin has been used as a food preservative for 6 decades with minimal development of resistance. Nisin contains the unusual amino acids dehydroalanine and dehydrobutyrine, which are posttranslationally installed by class I lanthipeptide dehydratases (LanBs) on a linear peptide substrate through an unusual glutamyl-tRNA-dependent dehydration of Ser and Thr. To date, little is known about how LanBs catalyze the transfer of glutamate from charged tRNA(Glu) to the peptide substrate, or how they carry out the subsequent elimination of the peptide-glutamyl adducts to afford dehydro amino acids. Here, we describe the synthesis of inert analogs that mimic substrate glutamyl-tRNA(Glu) and the glutamylated peptide intermediate, and determine the crystal structures of 2 LanBs in complex with each of these compounds. Mutational studies were used to characterize the function of the glutamylation and glutamate elimination active-site residues identified through the structural analysis. These combined studies provide insights into the mechanisms of substrate recognition, glutamylation, and glutamate elimination by LanBs to effect a net dehydration reaction of Ser and Thr. Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.,Bothwell IR, Cogan DP, Kim T, Reinhardt CJ, van der Donk WA, Nair SK Proc Natl Acad Sci U S A. 2019 Aug 13. pii: 1905240116. doi:, 10.1073/pnas.1905240116. PMID:31409709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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