2cc1
From Proteopedia
(New page: 200px<br /><applet load="2cc1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cc1, resolution 2.13Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2cc1.gif|left|200px]]<br /><applet load="2cc1" size=" | + | [[Image:2cc1.gif|left|200px]]<br /><applet load="2cc1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cc1, resolution 2.13Å" /> | caption="2cc1, resolution 2.13Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMASE FROM MYCOBACTERIUM FORTUITUM'''<br /> | '''CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMASE FROM MYCOBACTERIUM FORTUITUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | beta-Lactamases are the main cause of bacterial resistance to penicillins | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2CC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure | + | 2CC1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure supersedes 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2CC1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: penicillin]] | [[Category: penicillin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:17 2008'' |
Revision as of 14:47, 21 February 2008
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CRYSTAL STRUCTURE OF THE CLASS A BETA-LACTAMASE FROM MYCOBACTERIUM FORTUITUM
Overview
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.
About this Structure
2CC1 is a Single protein structure of sequence from [1]. This structure supersedes the now removed PDB entry 1MFO. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
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
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