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4a52
From Proteopedia
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| - | [[Image:4a52.jpg|left|200px]] | ||
| - | + | ==NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis== | |
| - | + | <StructureSection load='4a52' size='340' side='right'caption='[[4a52]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4a52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacsu Bacsu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A52 FirstGlance]. <br> | |
| - | or | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IM2:(5R)-5-[(1S,2R)-1-FORMYL-2-HYDROXYPROPYL]-3-[(2-{[(E)-IMINOMETHYL]AMINO}ETHYL)SULFANYL]-4,5-DIHYDRO-1H-PYRROLE-2-CARBOXYLIC+ACID'>IM2</scene></td></tr> |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1y7m|1y7m]], [[3zqd|3zqd]], [[4a1i|4a1i]], [[4a1j|4a1j]], [[4a1k|4a1k]]</div></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=4a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a52 OCA], [https://pdbe.org/4a52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a52 RCSB], [https://www.ebi.ac.uk/pdbsum/4a52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a52 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/YKUD_BACSU YKUD_BACSU]] Probable enzyme that may play an important role in cell wall biology.<ref>PMID:16287140</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | beta-lactams inhibit peptidoglycan polymerization by acting as suicide substrates of essential d,d-transpeptidases. Bypass of these enzymes by unrelated l,d-transpeptidases results in beta-lactam resistance, although carbapenems remain unexpectedly active. To gain insight into carbapenem specificity of l,d-transpeptidases (Ldts), we solved the nuclear magnetic resonance (NMR) structures of apo and imipenem-acylated Bacillus subtilis Ldt and show that the cysteine nucleophile is present as a neutral imidazole-sulfhydryl pair in the substrate-free enzyme. NMR relaxation dispersion does not reveal any preexisting conformational exchange in the apoenzyme, and change in flexibility is not observed upon noncovalent binding of beta-lactams (K(D) > 37.5 mM). In contrast, covalent modification of active cysteine by both carbapenems and 2-nitro-5-thiobenzoate induces backbone flexibility that does not result from disruption of the imidazole-sulfhydryl proton interaction or steric hindrance. The chemical step of the reaction determines enzyme specificity since no differences in drug affinity were observed. | ||
| - | + | Dynamics Induced by beta-Lactam Antibiotics in the Active Site of Bacillus subtilisl,d-Transpeptidase.,Lecoq L, Bougault C, Hugonnet JE, Veckerle C, Pessey O, Arthur M, Simorre JP Structure. 2012 May 9;20(5):850-61. PMID:22579252<ref>PMID:22579252</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4a52" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Bacsu]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Arthur, M]] | |
| - | == | + | [[Category: Bougault, C]] |
| - | < | + | [[Category: Hugonnet, J]] |
| - | [[Category: | + | [[Category: Lecoq, L]] |
| - | [[Category: Arthur, M | + | [[Category: Pessey, O]] |
| - | [[Category: Bougault, C | + | [[Category: Simorre, J]] |
| - | [[Category: Hugonnet, J | + | [[Category: Veckerle, C]] |
| - | [[Category: Lecoq, L | + | |
| - | [[Category: Pessey, O | + | |
| - | [[Category: Simorre, J | + | |
| - | [[Category: Veckerle, C | + | |
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
[[Category: Cysteine protease]] | [[Category: Cysteine protease]] | ||
[[Category: Peptidoglycan]] | [[Category: Peptidoglycan]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Current revision
NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis
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