X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.

@article{Munih2007XrayCC,
  title={X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica.},
  author={Petra Munih and Aaron Moulin and Carin C. Stamper and Brian J Bennett and Dagmar Ringe and Gregory A. Petsko and Richard C Holz},
  journal={Journal of inorganic biochemistry},
  year={2007},
  volume={101 8},
  pages={
          1099-107
        }
}
The X-ray crystal structure of the Co(II)-loaded form of the aminopeptidase from Aeromonas proteolytica ([CoCo(AAP)]) was solved to 2.2A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Co(II) binding to AAP does not introduce any major conformational changes to the overall protein structure and the amino acid residues ligated to the dicobalt(II) cluster in [CoCo(AAP)] are the… CONTINUE READING