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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 α-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.

Supporting information

PDB reference: AmpCD, 2zj9, r2zj9sf


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