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1zkj

From Proteopedia

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(New page: 200px<br /><applet load="1zkj" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zkj, resolution 1.55&Aring;" /> '''Structural Basis for...)
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[[Image:1zkj.gif|left|200px]]<br /><applet load="1zkj" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zkj, resolution 1.55&Aring;" />
 
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'''Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase'''<br />
 
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==Overview==
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==Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase==
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The emergence and dissemination of extended-spectrum (ES) beta-lactamases, induce therapeutic failure and a lack of eradication of clinical isolates, even by third-generation beta-lactam antibiotics like ceftazidime. CMY-10, is a plasmid-encoded class C beta-lactamase with a wide spectrum of, substrates. Unlike the well-studied class C ES beta-lactamase from, Enterobacter cloacae GC1, the Omega-loop does not affect the active site, conformation and the catalytic activity of CMY-10. Instead, a, three-amino-acid deletion in the R2-loop appears to be responsible for the, ES activity of CMY-10. According to the crystal structure solved at 1.55 A, resolution, the deletion significantly widens the R2 active site, which, accommodates the R2 side-chains of beta-lactam antibiotics. This, observation led us to demonstrate the hydrolysing activity of CMY-10, towards imipenem with a long R2 substituent. The forced mutational, analyses of P99 beta-lactamase reveal that the introduction of deletion, mutations into the R2-loop is able to extend the substrate spectrum of, class C non-ES beta-lactamases, which is compatible with the isolation of, natural class C ES enzymes harbouring deletion mutations in the R2-loop., Consequently, the opening of the R2 active site by the deletion of some, residues in the R2-loop can be considered as an operative molecular, strategy of class C beta-lactamases to extend their substrate spectrum.
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<StructureSection load='1zkj' size='340' side='right'caption='[[1zkj]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zkj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZKJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkj OCA], [https://pdbe.org/1zkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zkj RCSB], [https://www.ebi.ac.uk/pdbsum/1zkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zkj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q99QC1_KLEAE Q99QC1_KLEAE] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.[ARBA:ARBA00003808]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zk/1zkj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zkj ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ZKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_aerogenes Enterobacter aerogenes] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKJ OCA].
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase., Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, Lee KJ, Suh PG, Lee HS, Lee SH, Cha SS, Mol Microbiol. 2006 May;60(4):907-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16677302 16677302]
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[[Category: Klebsiella aerogenes]]
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[[Category: Beta-lactamase]]
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[[Category: Large Structures]]
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[[Category: Enterobacter aerogenes]]
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[[Category: An YJ]]
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[[Category: Single protein]]
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[[Category: Cha SS]]
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[[Category: An, Y.J.]]
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[[Category: Jung HI]]
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[[Category: Cha, S.S.]]
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[[Category: Lee SH]]
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[[Category: Jung, H.I.]]
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[[Category: Lee, S.H.]]
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[[Category: ACY]]
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[[Category: ZN]]
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[[Category: class c]]
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[[Category: cmy-10]]
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[[Category: extended spectrum beta-lactamase]]
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[[Category: plasmid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:36:54 2008''
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Current revision

Structural Basis for the Extended Substrate Spectrum of CMY-10, a Plasmid-Encoded Class C beta-lactamase

PDB ID 1zkj

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