Download MendeleyStructure of the SHV-1 beta-lactamase.
Kuzin, A.P., Nukaga, M., Nukaga, Y., Hujer, A.M., Bonomo, R.A., Knox, J.R.(1999) Biochemistry 38: 5720-5727
- PubMed: 10231522
- DOI: https://doi.org/10.1021/bi990136d
- Primary Citation of Related Structures:
1SHV - PubMed Abstract:
The X-ray crystallographic structure of the SHV-1 beta-lactamase has been established. The enzyme crystallizes from poly(ethylene glycol) at pH 7 in space group P212121 with cell dimensions a = 49.6 A, b = 55.6 A, and c = 87.0 A. The structure was solved by the molecular replacement method, and the model has been refined to an R-factor of 0.18 for all data in the range 8.0-1.98 A resolution. Deviations of model bonds and angles from ideal values are 0.018 A and 1.8 degrees, respectively. Overlay of all 263 alpha-carbon atoms in the SHV-1 and TEM-1 beta-lactamases results in an rms deviation of 1.4 A. Largest deviations occur in the H10 helix (residues 218-224) and in the loops between strands in the beta-sheet. All atoms in residues 70, 73, 130, 132, 166, and 234 in the catalytic site of SHV-1 deviate only 0.23 A (rms) from atoms in TEM-1. However, the width of the substrate binding cavity in SHV-1, as measured from the 104-105 and 130-132 loops on one side to the 235-238 beta-strand on the other side, is 0.7-1.2 A wider than in TEM-1. A structural analysis of the highly different affinity of SHV-1 and TEM-1 for the beta-lactamase inhibitory protein BLIP focuses on interactions involving Asp/Glu104.
Organizational Affiliation:
Department of Molecular and Cell Biology, The University of Connecticut, Storrs 06269-3125, USA.
