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| [[Image:1shv.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1shv| PDB=1shv | SCENE= }} | | {{STRUCTURE_1shv| PDB=1shv | SCENE= }} |
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| '''STRUCTURE OF SHV-1 BETA-LACTAMASE'''
| | ===STRUCTURE OF SHV-1 BETA-LACTAMASE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10231522}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10231522 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10231522}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Drug design]] | | [[Category: Drug design]] |
| [[Category: Penicillinase]] | | [[Category: Penicillinase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:43:26 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:40:38 2008'' |