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3kuv
From Proteopedia
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==Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with acetate.== | ==Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with acetate.== | ||
| - | <StructureSection load='3kuv' size='340' side='right' caption='[[3kuv]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3kuv' size='340' side='right'caption='[[3kuv]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3kuv]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3kuv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KUV FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3kuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kuv OCA], [https://pdbe.org/3kuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kuv RCSB], [https://www.ebi.ac.uk/pdbsum/3kuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kuv ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FLK_STRCT FLK_STRCT] Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Can not use acetyl-CoA as substrate.<ref>PMID:16720268</ref> <ref>PMID:20836570</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/3kuv_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/3kuv_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=3kuv ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3kuv" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Thioesterase|Thioesterase]] | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Streptomyces cattleya]] | [[Category: Streptomyces cattleya]] | ||
| - | [[Category: Blundell | + | [[Category: Blundell TL]] |
| - | [[Category: Chirgadze | + | [[Category: Chirgadze DY]] |
| - | [[Category: Dias | + | [[Category: Dias MVB]] |
| - | [[Category: Huang | + | [[Category: Huang F]] |
| - | [[Category: Leadlay | + | [[Category: Leadlay PF]] |
| - | [[Category: Spencer | + | [[Category: Spencer JB]] |
| - | [[Category: Spiteller | + | [[Category: Spiteller D]] |
| - | [[Category: Tosin | + | [[Category: Tosin M]] |
| - | [[Category: Valentine | + | [[Category: Valentine EF]] |
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Current revision
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with acetate.
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