Reference : Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basi...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/78082
Crystal structure of the Mycobacterium fortuitum class A beta-lactamase: structural basis for broad substrate specificity.
English
Sauvage, Eric mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Fonze, Eveline [> > > >]
Quinting, Birgit [> > > >]
Galleni, Moreno mailto [Université de Liège - ULg > Département des sciences de la vie > Macromolécules biologiques >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Charlier, Paulette mailto [Université de Liège - ULg > Département des sciences de la vie > Cristallographie des macromolécules biologiques >]
2006
Antimicrobial Agents and Chemotherapy
American Society for Microbiology (ASM)
50
7
2516-21
Yes (verified by ORBi)
International
0066-4804
1098-6596
Washington
DC
[en] Amino Acid Sequence ; Anti-Bacterial Agents/metabolism ; Binding Sites ; Cefotaxime/metabolism ; Crystallization ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium fortuitum/drug effects/enzymology ; Structure-Activity Relationship ; Substrate Specificity ; beta-Lactamases/chemistry/metabolism
[en] 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.
http://hdl.handle.net/2268/78082
10.1128/AAC.01226-05

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