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3byd
From Proteopedia
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| - | [[Image:3byd.png|left|200px]] | ||
| - | + | ==Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca== | |
| + | <StructureSection load='3byd' size='340' side='right'caption='[[3byd]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3byd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BYD 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]] 1.93Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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=3byd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byd OCA], [https://pdbe.org/3byd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3byd RCSB], [https://www.ebi.ac.uk/pdbsum/3byd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3byd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BLO1_KLEOX BLO1_KLEOX] Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins. | ||
| + | == 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/by/3byd_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=3byd ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Klebsiella oxytoca is a pathogen that causes serious infections in hospital patients. It shows resistance to many clinically used beta-lactam antibiotics by producing chromosomally encoded OXY-family beta-lactamases. Here, the crystal structure of an OXY-family beta-lactamase, OXY-1-1, determined at 1.93 A resolution is reported. The structure shows that the OXY-1-1 beta-lactamase has a typical class A beta-lactamase fold and exhibits greater similarity to CTX-M-type beta-lactamases than to TEM-family or SHV-family beta-lactamases. It is also shown that the enzyme provides more space around the active cavity for the R(1) and R(2) substituents of beta-lactam antibiotics. The half-positive/half-negative distribution of surface electrostatic potential in the substrate-binding pocket indicates the preferred properties of substrates or inhibitors of the enzyme. The results reported here provide a structural basis for the broadened substrate profile of the OXY-family beta-lactamases. | ||
| - | + | Structural insights into the broadened substrate profile of the extended-spectrum beta-lactamase OXY-1-1 from Klebsiella oxytoca.,Liang YH, Gao R, Su XD Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1460-7. doi:, 10.1107/S090744491203466X. Epub 2012 Oct 18. PMID:23090395<ref>PMID:23090395</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3byd" style="background-color:#fffaf0;"></div> | |
==See Also== | ==See Also== | ||
| - | *[[Beta-lactamase|Beta-lactamase]] | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Klebsiella oxytoca]] | [[Category: Klebsiella oxytoca]] | ||
| - | [[Category: Liang | + | [[Category: Large Structures]] |
| - | [[Category: Su | + | [[Category: Liang Y-H]] |
| - | [[Category: Wu | + | [[Category: Su X-D]] |
| - | + | [[Category: Wu SW]] | |
| - | + | ||
Current revision
Crystal structure of beta-lactamase OXY-1-1 from Klebsiella oxytoca
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