1shv

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[[Image:1shv.jpg|left|200px]]<br /><applet load="1shv" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1shv, resolution 1.98&Aring;" />
 
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'''STRUCTURE OF SHV-1 BETA-LACTAMASE'''<br />
 
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==Overview==
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==STRUCTURE OF SHV-1 BETA-LACTAMASE==
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<StructureSection load='1shv' size='340' side='right'caption='[[1shv]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1shv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SHV FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MA4:CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE'>MA4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1shv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shv OCA], [https://pdbe.org/1shv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1shv RCSB], [https://www.ebi.ac.uk/pdbsum/1shv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1shv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLA1_KLEPN BLA1_KLEPN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sh/1shv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1shv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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 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.
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==About this Structure==
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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<ref>PMID:10231522</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10231522 10231522]
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</div>
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[[Category: Beta-lactamase]]
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<div class="pdbe-citations 1shv" style="background-color:#fffaf0;"></div>
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[[Category: Klebsiella pneumoniae]]
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[[Category: Single protein]]
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[[Category: Bonomo, R A.]]
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[[Category: Hujer, A.]]
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[[Category: Knox, J R.]]
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[[Category: Kuzin, A P.]]
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[[Category: Nukaga, M.]]
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[[Category: Nukaga, Y.]]
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[[Category: MA4]]
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[[Category: beta-lactam hydrolase]]
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[[Category: detergent binding]]
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[[Category: drug design]]
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[[Category: penicillinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:39 2008''
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==See Also==
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Klebsiella pneumoniae]]
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[[Category: Large Structures]]
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[[Category: Bonomo RA]]
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[[Category: Hujer A]]
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[[Category: Knox JR]]
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[[Category: Kuzin AP]]
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[[Category: Nukaga M]]
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[[Category: Nukaga Y]]

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STRUCTURE OF SHV-1 BETA-LACTAMASE

PDB ID 1shv

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