Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.

@article{Fabiane1998CrystalSO,
  title={Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.},
  author={Stella Fabiane and Maninder K. Sohi and Tao Wan and David J Payne and John H. Bateson and Theresa Mitchell and Brian J. Sutton},
  journal={Biochemistry},
  year={1998},
  volume={37 36},
  pages={
          12404-11
        }
}
The structure of the zinc-dependent beta-lactamase II from Bacillus cereus has been determined at 1.9 A resolution in a crystal form with two molecules in the asymmetric unit and 400 waters (space group P3121; Rcryst = 20.8%). The active site contains two zinc ions: Zn1 is tightly coordinated by His86, His88, and His149, while Zn2 is loosely coordinated by Asp90, Cys168, and His210. A water molecule (W1) lies between the two zinc ions but is significantly closer to Zn1 and at a distance of only… CONTINUE READING
Highly Cited
This paper has 40 citations. REVIEW CITATIONS

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 18 citations