2l9x
From Proteopedia
(Difference between revisions)
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<StructureSection load='2l9x' size='340' side='right' caption='[[2l9x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2l9x' size='340' side='right' caption='[[2l9x]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2l9x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_95/8201 Bacillus cereus 95/8201]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9X OCA]. <br> | + | <table><tr><td colspan='2'>[[2l9x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus_95/8201 Bacillus cereus 95/8201]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9X OCA]. <br> |
| - | <b>[[Non-Standard_Residue|NonStd Res:]]</b> <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>< | + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTH:D-THREONINE'>DTH</scene></td></tr> |
| - | <b>[[Related_structure|Related:]]</b> [[2la0|2la0]]< | + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2la0|2la0]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9x RCSB], [http://www.ebi.ac.uk/pdbsum/2l9x PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l9x RCSB], [http://www.ebi.ac.uk/pdbsum/2l9x PDBsum]</span></td></tr> |
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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). | 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). | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:36, 1 May 2014
Trn- peptide of the two-component bacteriocin Thuricin CD
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