2cc1: Difference between revisions
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<StructureSection load='2cc1' size='340' side='right'caption='[[2cc1]], [[Resolution|resolution]] 2.13Å' scene=''> | <StructureSection load='2cc1' size='340' side='right'caption='[[2cc1]], [[Resolution|resolution]] 2.13Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.13Å</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=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> | <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> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BLAF_MYCFO BLAF_MYCFO] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycolicibacterium fortuitum]] | ||
[[Category: | [[Category: Charlier P]] | ||
[[Category: | [[Category: Fonze E]] | ||
[[Category: | [[Category: Sauvage E]] | ||
Latest revision as of 17:12, 13 December 2023
Crystal structure of the class A beta-lactamase from Mycobacterium fortuitumCrystal structure of the class A beta-lactamase from Mycobacterium fortuitum
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedbeta-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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