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| | ==NMR structure of the catalytic domain from E. faecium L,D- transpeptidase== | | ==NMR structure of the catalytic domain from E. faecium L,D- transpeptidase== |
| - | <StructureSection load='3zg4' size='340' side='right' caption='[[3zg4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='3zg4' size='340' side='right'caption='[[3zg4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zg4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19434 Atcc 19434]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZG4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZG4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zgp|3zgp]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidyltransferase Peptidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.12 2.3.2.12] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zg4 OCA], [https://pdbe.org/3zg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zg4 RCSB], [https://www.ebi.ac.uk/pdbsum/3zg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zg4 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zg4 OCA], [http://pdbe.org/3zg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zg4 RCSB], [http://www.ebi.ac.uk/pdbsum/3zg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zg4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q3Y185_ENTFD Q3Y185_ENTFD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 19434]] | + | [[Category: Enterococcus faecium]] |
| - | [[Category: Peptidyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Arthur, M]] | + | [[Category: Arthur M]] |
| - | [[Category: Bougault, C]] | + | [[Category: Bougault C]] |
| - | [[Category: Dubee, V]] | + | [[Category: Dubee V]] |
| - | [[Category: Hugonnet, J E]] | + | [[Category: Hugonnet JE]] |
| - | [[Category: Lecoq, L]] | + | [[Category: Lecoq L]] |
| - | [[Category: Simorre, J P]] | + | [[Category: Simorre JP]] |
| - | [[Category: Triboulet, S]] | + | [[Category: Triboulet S]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Peptidoglycan biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transpeptidation]]
| + | |
| Structural highlights
Function
Q3Y185_ENTFD
Publication Abstract from PubMed
The maintenance of bacterial cell shape and integrity is largely attributed to peptidoglycan, a biopolymer highly cross-linked through d,d-transpeptidation. Peptidoglycan cross-linking is catalyzed by penicillin-binding proteins (PBPs) that are the essential target of beta-lactam antibiotics. PBPs are functionally replaced by l,d-transpeptidases (Ldts) in ampicillin-resistant mutants of Enterococcus faecium and in wild-type Mycobacterium tuberculosis. Ldts are inhibited in vivo by a single class of beta-lactams, the carbapenems, which act as a suicide substrate. We present here the first structure of a carbapenem-acylated l,d-transpeptidase, E. faecium Ldtfm acylated by ertapenem, which revealed key contacts between the carbapenem core and residues of the catalytic cavity of the enzyme. Significant reorganization of the antibiotic conformation occurs upon enzyme acylation. These results, together with the analysis of protein-to-carbapenem proton transfers, provide new insights into the mechanism of Ldt acylation by carbapenems.
Structure of Enterococcus faeciuml,d-Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism.,Lecoq L, Dubee V, Triboulet S, Bougault C, Hugonnet JE, Arthur M, Simorre JP ACS Chem Biol. 2013 Apr 12. PMID:23574509[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lecoq L, Dubee V, Triboulet S, Bougault C, Hugonnet JE, Arthur M, Simorre JP. Structure of Enterococcus faeciuml,d-Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism. ACS Chem Biol. 2013 Apr 12. PMID:23574509 doi:10.1021/cb4001603
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