2LA0
Trn- peptide of the two-component bacteriocin Thuricin CD
Summary for 2LA0
| Entry DOI | 10.2210/pdb2la0/pdb |
| Related | 2L9X |
| NMR Information | BMRB: 17495 |
| Descriptor | Uncharacterized protein (1 entity in total) |
| Functional Keywords | thioether bridges, helical loops, crosslinked, post-translationally modified, antimicrobial protein |
| Biological source | Bacillus cereus 95/8201 |
| Total number of polymer chains | 1 |
| Total formula weight | 2868.27 |
| Authors | Sit, C.S.,Mckay, R.T.,Hill, C.,Ross, R.P.,Vederas, J.C. (deposition date: 2011-02-27, release date: 2012-01-11, Last modification date: 2024-10-30) |
| Primary citation | Sit, C.S.,McKay, R.T.,Hill, C.,Ross, R.P.,Vederas, J.C. The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links. J.Am.Chem.Soc., 133:7680-7683, 2011 Cited by PubMed Abstract: Thuricin CD is an antimicrobial factor that consists of two peptides, Trn-α and Trn-β, that exhibit synergistic activity against drug resistant strains of Clostridium difficile. Trn-α and Trn-β each possess three sulfur to α-carbon thioether bridges for which the stereochemistry is unknown. This report presents the three-dimensional solution structures of Trn-α and Trn-β. 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-α has L-stereochemistry at Ser21 (α-R), L-stereochemistry at Thr25 (α-R), and D-stereochemistry at Thr28 (α-S) (an LLD isomer). Trn-β was also found to be the LLD isomer, with L-stereochemistry at Thr21 (α-R), L-stereochemistry at Ala25 (α-R), and D-stereochemistry at Tyr28 (α-S). PubMed: 21526839DOI: 10.1021/ja201802f PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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