2la0

Trn- peptide of the two-component bacteriocin Thuricin CD

spinqualitylabelsall models 2la0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2la0 is a 1 chain structure with sequence from Bacillus cereus 95/8201. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: DTY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Thuricin CD is an antimicrobial factor that consists of two peptides, Trn-alpha and Trn-beta, that exhibit synergistic activity against drug resistant strains of Clostridium difficile. Trn-alpha and Trn-beta each possess three sulfur to alpha-carbon thioether bridges for which the stereochemistry is unknown. This report presents the three-dimensional solution structures of Trn-alpha and Trn-beta. Structure calculations were performed for the eight possible stereoisomers of each peptide based on the same NMR data. The structure of the stereoisomer that best fit the experimental data was chosen as the representative structure for each peptide. It was determined that Trn-alpha has L-stereochemistry at Ser21 (alpha-R), L-stereochemistry at Thr25 (alpha-R), and D-stereochemistry at Thr28 (alpha-S) (an LLD isomer). Trn-beta was also found to be the LLD isomer, with L-stereochemistry at Thr21 (alpha-R), L-stereochemistry at Ala25 (alpha-R), and D-stereochemistry at Tyr28 (alpha-S). The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links.,Sit CS, McKay RT, Hill C, Ross RP, Vederas JC J Am Chem Soc. 2011 May 25;133(20):7680-3. Epub 2011 Apr 28. PMID:21526839 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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