3p98: Difference between revisions
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==The crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrate== | |||
<StructureSection load='3p98' size='340' side='right'caption='[[3p98]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3p98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Morganella_morganii Morganella morganii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P98 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=3p98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p98 OCA], [https://pdbe.org/3p98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p98 RCSB], [https://www.ebi.ac.uk/pdbsum/3p98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p98 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9R429_MORMO Q9R429_MORMO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TEM-72, a class A beta-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum beta-lactamase (ESBL) properties arising from the G238S and E240K substitutions. Although many structures of TEM variants have been published, they do not include an enzyme with the simultaneous presence of both of the ESBL-conferring G238S and E240K substitutions. Furthermore, the structure shows the presence of a citrate anion bound to the TEM-72 active site, where it interacts with all of the conserved residues of class A beta-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine beta-lactamases. | |||
Structure of the extended-spectrum beta-lactamase TEM-72 inhibited by citrate.,Docquier JD, Benvenuti M, Calderone V, Rossolini GM, Mangani S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):303-6. Epub 2011 Feb 18. PMID:21393831<ref>PMID:21393831</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3p98" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Morganella morganii]] | [[Category: Morganella morganii]] | ||
[[Category: Benvenuti | [[Category: Benvenuti M]] | ||
[[Category: Calderone | [[Category: Calderone V]] | ||
[[Category: Docquier | [[Category: Docquier JD]] | ||
[[Category: Mangani | [[Category: Mangani S]] | ||
[[Category: Rossolini | [[Category: Rossolini GM]] | ||
Latest revision as of 12:50, 6 September 2023
The crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrateThe crystal structure of the extended spectrum beta-lactamase TEM-72 reveals inhibition by citrate
Structural highlights
FunctionPublication Abstract from PubMedTEM-72, a class A beta-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum beta-lactamase (ESBL) properties arising from the G238S and E240K substitutions. Although many structures of TEM variants have been published, they do not include an enzyme with the simultaneous presence of both of the ESBL-conferring G238S and E240K substitutions. Furthermore, the structure shows the presence of a citrate anion bound to the TEM-72 active site, where it interacts with all of the conserved residues of class A beta-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine beta-lactamases. Structure of the extended-spectrum beta-lactamase TEM-72 inhibited by citrate.,Docquier JD, Benvenuti M, Calderone V, Rossolini GM, Mangani S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):303-6. Epub 2011 Feb 18. PMID:21393831[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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