The X-ray crystal structure of AmpC β-lactamase (AmpCD) with a tripeptide deletion (Gly286-Ser287-Asp288) produced by Escherichia coli HKY28, a ceftazidime-resistant strain, was determined at a resolution of 1.7 Å. The structure of AmpCD suggests that the tripeptide deletion at positions 286-288 located in the H10 helix causes a structural change of the Asn289-Asn294 region from the -helix present in the native AmpC β-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.
|Number of pages||4|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - 10-07-2009|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Condensed Matter Physics