2cc1

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(New page: 200px<br /><applet load="2cc1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cc1, resolution 2.13&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:2cc1.gif|left|200px]]<br /><applet load="2cc1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cc1, resolution 2.13&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMASE FROM MYCOBACTERIUM FORTUITUM'''<br />
 
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==Overview==
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==Crystal structure of the class A beta-lactamase from Mycobacterium fortuitum==
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beta-Lactamases are the main cause of bacterial resistance to penicillins, and cephalosporins. Class A beta-lactamases, the largest group of, beta-lactamases, have been found in many bacterial strains, including, mycobacteria, for which no beta-lactamase structure has been previously, reported. The crystal structure of the class A beta-lactamase from, Mycobacterium fortuitum (MFO) has been solved at 2.13-A resolution. The, enzyme is a chromosomally encoded broad-spectrum beta-lactamase with low, specific activity on cefotaxime. Specific features of the active site of, the class A beta-lactamase from M. fortuitum are consistent with its, specificity profile. Arg278 and Ser237 favor cephalosporinase activity and, could explain its broad substrate activity. The MFO active site presents, similarities with the CTX-M type extended-spectrum beta-lactamases but, lacks a specific feature of these enzymes, the VNYN motif (residues 103 to, 106), which confers on CTX-M-type extended-spectrum beta-lactamases a more, efficient cefotaximase activity.
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<StructureSection load='2cc1' size='340' side='right'caption='[[2cc1]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_fortuitum Mycolicibacterium fortuitum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mfo 1mfo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CC1 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]] 2.13&#8491;</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=2cc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cc1 OCA], [https://pdbe.org/2cc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cc1 RCSB], [https://www.ebi.ac.uk/pdbsum/2cc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cc1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLAF_MYCFO BLAF_MYCFO]
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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/cc/2cc1_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=2cc1 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 are the main cause of bacterial resistance to penicillins and cephalosporins. Class A beta-lactamases, the largest group of beta-lactamases, have been found in many bacterial strains, including mycobacteria, for which no beta-lactamase structure has been previously reported. The crystal structure of the class A beta-lactamase from Mycobacterium fortuitum (MFO) has been solved at 2.13-A resolution. The enzyme is a chromosomally encoded broad-spectrum beta-lactamase with low specific activity on cefotaxime. Specific features of the active site of the class A beta-lactamase from M. fortuitum are consistent with its specificity profile. Arg278 and Ser237 favor cephalosporinase activity and could explain its broad substrate activity. The MFO active site presents similarities with the CTX-M type extended-spectrum beta-lactamases but lacks a specific feature of these enzymes, the VNYN motif (residues 103 to 106), which confers on CTX-M-type extended-spectrum beta-lactamases a more efficient cefotaximase activity.
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==About this Structure==
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Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.,Sauvage E, Fonze E, Quinting B, Galleni M, Frere JM, Charlier P Antimicrob Agents Chemother. 2006 Jul;50(7):2516-21. PMID:16801434<ref>PMID:16801434</ref>
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2CC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure superseeds the now removed PDB entry 1MFO. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CC1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity., Sauvage E, Fonze E, Quinting B, Galleni M, Frere JM, Charlier P, Antimicrob Agents Chemother. 2006 Jul;50(7):2516-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16801434 16801434]
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</div>
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[[Category: Beta-lactamase]]
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<div class="pdbe-citations 2cc1" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Charlier, P.]]
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[[Category: Fonze, E.]]
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[[Category: Sauvage, E.]]
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[[Category: antibiotic resistance]]
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[[Category: beta-lactamase]]
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[[Category: broad-spectrum]]
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[[Category: hydrolase]]
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[[Category: penicillin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:04:38 2007''
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycolicibacterium fortuitum]]
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[[Category: Charlier P]]
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[[Category: Fonze E]]
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[[Category: Sauvage E]]

Current revision

Crystal structure of the class A beta-lactamase from Mycobacterium fortuitum

PDB ID 2cc1

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