1SHV
STRUCTURE OF SHV-1 BETA-LACTAMASE
Summary for 1SHV
| Entry DOI | 10.2210/pdb1shv/pdb |
| Descriptor | PROTEIN (BETA-LACTAMASE SHV-1), CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE (3 entities in total) |
| Functional Keywords | beta-lactam hydrolase, penicillinase, detergent binding, drug design, hydrolase |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 29415.62 |
| Authors | Kuzin, A.P.,Nukaga, M.,Nukaga, Y.,Hujer, A.,Bonomo, R.A.,Knox, J.R. (deposition date: 1999-02-23, release date: 1999-05-06, Last modification date: 2024-11-13) |
| Primary citation | Kuzin, A.P.,Nukaga, M.,Nukaga, Y.,Hujer, A.M.,Bonomo, R.A.,Knox, J.R. Structure of the SHV-1 beta-lactamase. Biochemistry, 38:5720-5727, 1999 Cited by 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. PubMed: 10231522DOI: 10.1021/bi990136d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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