Structure of GES-1 at atomic resolution: insights into the evolution of carbapenamase activity in the class A extended-spectrum beta-lactamases.

@article{Smith2007StructureOG,
  title={Structure of GES-1 at atomic resolution: insights into the evolution of carbapenamase activity in the class A extended-spectrum beta-lactamases.},
  author={Clyde A. Smith and Marisa Caccamo and Katherine A. Kantardjieff and Sergei Vakulenko},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2007},
  volume={63 Pt 9},
  pages={982-92}
}
The structure of the class A extended-spectrum beta-lactamase GES-1 from Klebsiella pneumoniae has been determined to 1.1 A resolution. GES-1 has the characteristic active-site disulfide bond of the carbapenemase family of beta-lactamases and has a structure that is very similar to those of other known carbapenemases, including NMC-A, SME-1 and KPC-2. Most residues implicated in the catalytic mechanism of this class of enzyme are present in the GES-1 active site, including Ser70, which forms a… CONTINUE READING