Summary for 2CC1
| Entry DOI | 10.2210/pdb2cc1/pdb |
| Descriptor | Beta-lactamase (2 entities in total) |
| Functional Keywords | hydrolase, antibiotic resistance, beta-lactamase, broad-spectrum, penicillin |
| Biological source | Mycolicibacterium fortuitum |
| Total number of polymer chains | 1 |
| Total formula weight | 28108.68 |
| Authors | Sauvage, E.,Fonze, E.,Charlier, P. (deposition date: 2006-01-11, release date: 2006-01-13, Last modification date: 2023-12-13) |
| Primary citation | Sauvage, E.,Fonze, E.,Quinting, B.,Galleni, M.,Frere, J.M.,Charlier, P. Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity. Antimicrob. Agents Chemother., 50:2516-2521, 2006 Cited by PubMed Abstract: 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. PubMed: 16801434DOI: 10.1128/AAC.01226-05 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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