1shv
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STRUCTURE OF SHV-1 BETA-LACTAMASE
OverviewOverview
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.
About this StructureAbout this Structure
1SHV is a Single protein structure of sequence from Klebsiella pneumoniae with MA4 as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the SHV-1 beta-lactamase., Kuzin AP, Nukaga M, Nukaga Y, Hujer AM, Bonomo RA, Knox JR, Biochemistry. 1999 May 4;38(18):5720-7. PMID:10231522
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