Structural highlights
Publication Abstract from PubMed
TEM-72, a class A beta-lactamase identified in isolates of Enterobacteriaceae, is a quadruple mutant of TEM-1 (Q39K, M182T, G238S and E240K) and shows extended-spectrum beta-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 beta-lactamases. The present structure supports the use of polycarboxylates as a scaffold for the design of broad-spectrum inhibitors of serine beta-lactamases.
Structure of the extended-spectrum beta-lactamase TEM-72 inhibited by citrate.,Docquier JD, Benvenuti M, Calderone V, Rossolini GM, Mangani S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):303-6. Epub 2011 Feb 18. PMID:21393831[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Docquier JD, Benvenuti M, Calderone V, Rossolini GM, Mangani S. Structure of the extended-spectrum beta-lactamase TEM-72 inhibited by citrate. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):303-6. Epub 2011 Feb 18. PMID:21393831 doi:10.1107/S1744309110054680
