1shv: Difference between revisions

Revision as of 21:40, 28 July 2008

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File:1shv.png

Template:STRUCTURE 1shv

STRUCTURE OF SHV-1 BETA-LACTAMASESTRUCTURE OF SHV-1 BETA-LACTAMASE

Template:ABSTRACT PUBMED 10231522

About this StructureAbout this Structure

1SHV is a Single protein structure of sequence from Klebsiella pneumoniae. 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

Page seeded by OCA on Mon Jul 28 21:40:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''
+===STRUCTURE OF SHV-1 BETA-LACTAMASE===
-==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
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+{{ABSTRACT_PUBMED_10231522}}
 ==About this Structure==
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 [[Category: Drug design]]
 [[Category: Penicillinase]]
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