1kvm

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[[Image:1kvm.gif|left|200px]]
 
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{{Structure
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==X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin==
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|PDB= 1kvm |SIZE=350|CAPTION= <scene name='initialview01'>1kvm</scene>, resolution 2.06&Aring;
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<StructureSection load='1kvm' size='340' side='right'caption='[[1kvm]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CEO:5-METHYLENE-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC+ACID'>CEO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1kvm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KVM FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.06&#8491;</td></tr>
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|GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CEO:5-METHYLENE-2-[2-OXO-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-ETHYL]-5,6-DIHYDRO-2H-[1,3]THIAZINE-4-CARBOXYLIC+ACID'>CEO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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|DOMAIN=
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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=1kvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kvm OCA], [https://pdbe.org/1kvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kvm RCSB], [https://www.ebi.ac.uk/pdbsum/1kvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kvm ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1kvl|1KVL]], [[1ke4|1KE4]], [[2bls|2BLS]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kvm OCA], [http://www.ebi.ac.uk/pdbsum/1kvm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kvm RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
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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/kv/1kvm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kvm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Beta-lactamases hydrolyze beta-lactam antibiotics and are the leading cause of bacterial resistance to these drugs. Although beta-lactamases have been extensively studied, structures of the substrate-enzyme and product-enzyme complexes have proven elusive. Here, the structure of a mutant AmpC in complex with the beta-lactam cephalothin in its substrate and product forms was determined by X-ray crystallography to 1.53 A resolution. The acyl-enzyme intermediate between AmpC and cephalothin was determined to 2.06 A resolution. The ligand undergoes a dramatic conformational change as the reaction progresses, with the characteristic six-membered dihydrothiazine ring of cephalothin rotating by 109 degrees. These structures correspond to all three intermediates along the reaction path and provide insight into substrate recognition, catalysis, and product expulsion.
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'''X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin'''
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Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.,Beadle BM, Trehan I, Focia PJ, Shoichet BK Structure. 2002 Mar;10(3):413-24. PMID:12005439<ref>PMID:12005439</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kvm" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Beta-lactamases hydrolyze beta-lactam antibiotics and are the leading cause of bacterial resistance to these drugs. Although beta-lactamases have been extensively studied, structures of the substrate-enzyme and product-enzyme complexes have proven elusive. Here, the structure of a mutant AmpC in complex with the beta-lactam cephalothin in its substrate and product forms was determined by X-ray crystallography to 1.53 A resolution. The acyl-enzyme intermediate between AmpC and cephalothin was determined to 2.06 A resolution. The ligand undergoes a dramatic conformational change as the reaction progresses, with the characteristic six-membered dihydrothiazine ring of cephalothin rotating by 109 degrees. These structures correspond to all three intermediates along the reaction path and provide insight into substrate recognition, catalysis, and product expulsion.
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1KVM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVM OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase., Beadle BM, Trehan I, Focia PJ, Shoichet BK, Structure. 2002 Mar;10(3):413-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12005439 12005439]
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[[Category: Beta-lactamase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Beadle, B M.]]
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[[Category: Beadle BM]]
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[[Category: Focia, P J.]]
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[[Category: Focia PJ]]
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[[Category: Shoichet, B K.]]
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[[Category: Shoichet BK]]
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[[Category: Trehan, I.]]
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[[Category: Trehan I]]
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[[Category: acyl-enzyme complex]]
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[[Category: amide hydrolase]]
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[[Category: beta-lactamase]]
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[[Category: cephalothin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:54:11 2008''
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Current revision

X-ray Crystal Structure of AmpC WT beta-Lactamase in Complex with Covalently Bound Cephalothin

PDB ID 1kvm

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