4a52: Difference between revisions

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[[Image:4a52.jpg|left|200px]]


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==NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis==
The line below this paragraph, containing "STRUCTURE_4a52", creates the "Structure Box" on the page.
<StructureSection load='4a52' size='340' side='right'caption='[[4a52]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[4a52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<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>
{{STRUCTURE_4a52|  PDB=4a52  |  SCENE=  }}
<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) &gt; 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.


===NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
The line below this paragraph, {{ABSTRACT_PUBMED_22579252}}, adds the Publication Abstract to the page
<div class="pdbe-citations 4a52" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 22579252 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_22579252}}
__TOC__
 
</StructureSection>
==About this Structure==
[[4a52]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A52 OCA].
 
==Reference==
<ref group="xtra">PMID:022579252</ref><references group="xtra"/>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Arthur, M.]]
[[Category: Large Structures]]
[[Category: Bougault, C.]]
[[Category: Arthur M]]
[[Category: Hugonnet, J.]]
[[Category: Bougault C]]
[[Category: Lecoq, L.]]
[[Category: Hugonnet J]]
[[Category: Pessey, O.]]
[[Category: Lecoq L]]
[[Category: Simorre, J.]]
[[Category: Pessey O]]
[[Category: Veckerle, C.]]
[[Category: Simorre J]]
[[Category: Antibiotic resistance]]
[[Category: Veckerle C]]
[[Category: Cysteine protease]]
[[Category: Peptidoglycan]]
[[Category: Transferase]]

Latest revision as of 08:15, 23 October 2024

NMR structure of the imipenem-acylated L,D-transpeptidase from Bacillus subtilis

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