Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix

Acta Cryst. (2009). F65, 540–543 (doi.org/10.1107/S1744309109014249)

Pathogenic bacteria that produce AmpC β-lactamases are recognized as a serious threat because of their consistent resistance to various β-lactams. The crystal structure of AmpC β-lactamase (AmpCD) with a tripeptide deletion (Gly286-Ser287-Asp288) from E. coli located in the H10 helix was determined at 1.7 Å resolution. A comparison of the structures in AmpCD and native AmpC reveals that the deletion of the Gly286-Ser287-Asp288 residues causes the structural change from α-helix structure to a more extended loop, which results in an expansion of the binding pocket.

Y. Yamaguchi, G. Sato, Y. Yamagata, Y. Doi, J. Wachino, Y. Arakawa, K. Matsuda and H. Kurosaki