1shv
From Proteopedia
(New page: 200px<br /><applet load="1shv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1shv, resolution 1.98Å" /> '''STRUCTURE OF SHV-1 B...) |
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| - | [[Image:1shv.jpg|left|200px]]<br /><applet load="1shv" size=" | + | [[Image:1shv.jpg|left|200px]]<br /><applet load="1shv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1shv, resolution 1.98Å" /> | caption="1shv, resolution 1.98Å" /> | ||
'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''<br /> | '''STRUCTURE OF SHV-1 BETA-LACTAMASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystallographic structure of the SHV-1 beta-lactamase has been | + | 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== | ==About this Structure== | ||
| - | 1SHV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with MA4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1SHV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae] with <scene name='pdbligand=MA4:'>MA4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Klebsiella pneumoniae]] | [[Category: Klebsiella pneumoniae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bonomo, R | + | [[Category: Bonomo, R A.]] |
[[Category: Hujer, A.]] | [[Category: Hujer, A.]] | ||
| - | [[Category: Knox, J | + | [[Category: Knox, J R.]] |
| - | [[Category: Kuzin, A | + | [[Category: Kuzin, A P.]] |
[[Category: Nukaga, M.]] | [[Category: Nukaga, M.]] | ||
[[Category: Nukaga, Y.]] | [[Category: Nukaga, Y.]] | ||
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[[Category: penicillinase]] | [[Category: penicillinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:39 2008'' |
Revision as of 13:01, 21 February 2008
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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 with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 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
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