4a52: Difference between revisions
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==NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis== | ==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=''> | <StructureSection load='4a52' size='340' side='right' caption='[[4a52]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1y7m|1y7m]], [[3zqd|3zqd]], [[4a1i|4a1i]], [[4a1j|4a1j]], [[4a1k|4a1k]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y7m|1y7m]], [[3zqd|3zqd]], [[4a1i|4a1i]], [[4a1j|4a1j]], [[4a1k|4a1k]]</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=4a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a52 RCSB], [http://www.ebi.ac.uk/pdbsum/4a52 PDBsum]</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=4a52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a52 OCA], [http://pdbe.org/4a52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a52 RCSB], [http://www.ebi.ac.uk/pdbsum/4a52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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> | </div> | ||
<div class="pdbe-citations 4a52" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:53, 4 August 2016
NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilisNMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis
Structural highlights
Function[YKUD_BACSU] Probable enzyme that may play an important role in cell wall biology.[1] Publication Abstract from PubMedbeta-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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