This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3kuv
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==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 [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3kuv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_cattleya"_kahan_et_al._1979 "streptomyces cattleya" kahan et al. 1979]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KUV FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kuw|3kuw]], [[3kv7|3kv7]], [[3kv8|3kv8]], [[3kvi|3kvi]], [[3kvu|3kvu]], [[3kvz|3kvz]], [[3kw1|3kw1]], [[3kx7|3kx7]], [[3kx8|3kx8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kuw|3kuw]], [[3kv7|3kv7]], [[3kv8|3kv8]], [[3kvi|3kvi]], [[3kvu|3kvu]], [[3kvz|3kvz]], [[3kw1|3kw1]], [[3kx7|3kx7]], [[3kx8|3kx8]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flK, fluoroacetyl-CoA thioesterase FlK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 Streptomyces cattleya])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">flK, fluoroacetyl-CoA thioesterase FlK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29303 "Streptomyces cattleya" Kahan et al. 1979])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kuv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kuv RCSB], [http://www.ebi.ac.uk/pdbsum/3kuv PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kuv OCA], [http://pdbe.org/3kuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kuv RCSB], [http://www.ebi.ac.uk/pdbsum/3kuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kuv ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://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]] | ||
| Line 18: | Line 19: | ||
<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;"> | ||
| Line 28: | Line 29: | ||
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== | ||
| Line 35: | Line 37: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Streptomyces cattleya]] | + | [[Category: Streptomyces cattleya kahan et al. 1979]] |
[[Category: Blundell, T L]] | [[Category: Blundell, T L]] | ||
[[Category: Chirgadze, D Y]] | [[Category: Chirgadze, D Y]] | ||
Revision as of 09:29, 4 August 2016
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - T42S mutant in complex with acetate.
| |||||||||||
