2zq8
From Proteopedia
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| - | [[Image:2zq8.png|left|200px]] | ||
| - | + | ==Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant== | |
| + | <StructureSection load='2zq8' size='340' side='right'caption='[[2zq8]], [[Resolution|resolution]] 1.03Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2zq8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZQ8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.03Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zq8 OCA], [https://pdbe.org/2zq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zq8 RCSB], [https://www.ebi.ac.uk/pdbsum/2zq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zq8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zq/2zq8_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2zq8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The beta-lactamase Toho-1 exhibits a strong tendency to form merohedrally twinned crystals. Here, the crystal quality of Toho-1 was improved by using surface modification to remove a sulfate ion involved in crystal packing. The surface-modified Toho-1 variant (R274N/R276N) was crystallized under similar conditions to those used for wild-type Toho-1. R274N/R276N did not form merohedrally twinned crystals. The crystals diffracted to a significantly higher resolution (approximately 0.97 A) than the wild-type crystals (1.65 A); they belonged to the same space group and had almost identical unit-cell parameters to those of wild-type Toho-1. | ||
| - | + | Improvement of crystal quality by surface mutations of beta-lactamase Toho-1.,Shimamura T, Nitanai Y, Uchiyama T, Matsuzawa H Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt, 4):379-82. Epub 2009 Mar 25. PMID:19342785<ref>PMID:19342785</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2zq8" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Beta-lactamase|Beta-lactamase]] | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Ago | + | [[Category: Large Structures]] |
| - | [[Category: Matsuzawa | + | [[Category: Ago H]] |
| - | [[Category: Miyano | + | [[Category: Matsuzawa H]] |
| - | [[Category: Nitanai | + | [[Category: Miyano M]] |
| - | [[Category: Shimamura | + | [[Category: Nitanai Y]] |
| - | [[Category: Uchiyama | + | [[Category: Shimamura T]] |
| - | + | [[Category: Uchiyama T]] | |
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Current revision
Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant
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