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

Jean Denis Docquier, Manuela Benvenuti, Vito Calderone, Gian Maria Rossolini, Stefano Mangani

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)303-306
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number3
Publication statusPublished - Mar 2011


  • citrate
  • class A β-lactamases
  • extended-spectrum β-lactamases
  • inhibitors
  • polycarboxylate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics


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