Peer-Reviewed Journal Details
Mandatory Fields
Sit, CS;Mckay, RT;Hill, C;Ross, RP;Vederas, JC
2011
May
Journal of the American Chemical Society
The 3D Structure of Thuricin CD, a Two-Component Bacteriocin with Cysteine Sulfur to alpha-Carbon Cross-links
Validated
WOS: 40 ()
Optional Fields
AMINO-ACID-SEQUENCE BACILLUS-THURINGIENSIS SUBTILOSIN-A ANTIMICROBIAL PEPTIDE PURIFICATION
133
7680
7683
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).
WASHINGTON
0002-7863
10.1021/ja201802f
Grant Details