2ZJ9

X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a Tripeptide Deletion (Gly286 Ser287 Asp288) on the H10 Helix

Summary for 2ZJ9

• Entry DOI: 10.2210/pdb2zj9/pdb
• Descriptor: AmpC, SODIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total)
• Functional Keywords: lactamase, tripeptide deletion, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 79022.11

Authors

Yamaguchi, Y.,Sato, G.,Yamagata, Y.,Wachino, J.,Arakawa, Y.,Kurosaki, H. (deposition date: 2008-02-29, release date: 2009-03-10, Last modification date: 2023-11-01)

Primary citation

Yamaguchi, Y.,Sato, G.,Yamagata, Y.,Doi, Y.,Wachino, J.,Arakawa, Y.,Matsuda, K.,Kurosaki, H.
Structure of AmpC beta-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix
Acta Crystallogr.,Sect.F, 65:540-543, 2009

PubMed Abstract: The X-ray crystal structure of AmpC beta-lactamase (AmpC(D)) with a tripeptide deletion (Gly286-Ser287-Asp288) produced by Escherichia coli HKY28, a ceftazidime-resistant strain, was determined at a resolution of 1.7 A. The structure of AmpC(D) 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 alpha-helix present in the native AmpC beta-lactamase of E. coli to a loop structure, which results in a widening of the substrate-binding site.

PubMed: 19478427
DOI: 10.1107/S1744309109014249

Experimental method

X-RAY DIFFRACTION (1.7 Å)