1shv

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[[Image:1shv.jpg|left|200px]]
[[Image:1shv.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1shv |SIZE=350|CAPTION= <scene name='initialview01'>1shv</scene>, resolution 1.98&Aring;
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The line below this paragraph, containing "STRUCTURE_1shv", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= BLA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 Klebsiella pneumoniae])
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-->
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|DOMAIN=
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{{STRUCTURE_1shv| PDB=1shv | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1shv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shv OCA], [http://www.ebi.ac.uk/pdbsum/1shv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1shv RCSB]</span>
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}}
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'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''
'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''
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[[Category: Nukaga, M.]]
[[Category: Nukaga, M.]]
[[Category: Nukaga, Y.]]
[[Category: Nukaga, Y.]]
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[[Category: beta-lactam hydrolase]]
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[[Category: Beta-lactam hydrolase]]
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[[Category: detergent binding]]
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[[Category: Detergent binding]]
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[[Category: drug design]]
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[[Category: Drug design]]
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[[Category: penicillinase]]
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[[Category: Penicillinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:43:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:42:15 2008''
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Revision as of 05:43, 3 May 2008

Image:1shv.jpg

Template:STRUCTURE 1shv

STRUCTURE OF SHV-1 BETA-LACTAMASE


Overview

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 Structure

1SHV is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 08:43:26 2008

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