Structure of AmpC β-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix
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
![[AmpC beta-lactamase]](https://www.iucr.org/__data/assets/image/0013/26104/ActaF.jpg)
Slabbed view of overall structure superposition of native AmpC β-lactamase (red) (PDB code 1KE4) and AmpCD β-lactamase (blue) (PDB code 2ZJ9).
