Structure of the extended-spectrum β-lactamase TEM-72 inhibited by citrate

[en] TEM-72, a class A β-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum β-lactamase (ESBL) properties arising from the G238S and E240K substitutions. Although many structures of TEM variants have been published, they do not include an enzyme with the simultaneous presence of both of the ESBL-conferring G238S and E240K substitutions. Furthermore, the structure shows the presence of a citrate anion bound to the TEM-72 active site, where it interacts with all of the conserved residues of class A β-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine β-lactamases. © 2011 International Union of Crystallography All rights reserved.

Disciplines :

Life sciences: Multidisciplinary, general & others
Biochemistry, biophysics & molecular biology
Microbiology

Author, co-author :

Docquier, Jean-Denis ; Université de Liège - ULiège > Département des sciences de la vie > Centre d'ingénierie des protéines

Benvenuti, M.; Dipartimento di Chimica, Universitá di Siena, Siena I-53100, Italy

Calderone, V.; Magnetic Resonance Center CERM, Universitá di Firenze, Sesto Fiorentino I-50019, Italy

Rossolini, G.-M.; Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia Dei Microrganismi, Universitá di Siena, Siena I-53100, Italy, U. O. C. Microbiologia e Virologia, Universitá di Siena, Siena I-53100, Italy

Mangani, S.; Dipartimento di Chimica, Universitá di Siena, Siena I-53100, Italy, Magnetic Resonance Center CERM, Universitá di Firenze, Sesto Fiorentino I-50019, Italy

Language :

English

Title :

Structure of the extended-spectrum β-lactamase TEM-72 inhibited by citrate

Publication date :

2011

Journal title :

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

eISSN :

1744-3091

Publisher :

International Union of Crystallography, United Kingdom

Volume :

Issue :

Pages :

303-306

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 20 November 2020

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