1q4t: Difference between revisions
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='1q4t' size='340' side='right' caption='[[1q4t]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1q4t' size='340' side='right' caption='[[1q4t]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1q4t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q4T FirstGlance]. <br> | <table><tr><td colspan='2'>[[1q4t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp._dsm20407 Arthrobacter sp. dsm20407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q4T FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CO:4-HYDROXYPHENACYL+COENZYME+A'>4CO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CO:4-HYDROXYPHENACYL+COENZYME+A'>4CO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q4s|1q4s]], [[1q4u|1q4u]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q4s|1q4s]], [[1q4u|1q4u]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=71255 Arthrobacter sp. DSM20407])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] </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=1q4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q4t RCSB], [http://www.ebi.ac.uk/pdbsum/1q4t 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=1q4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4t OCA], [http://pdbe.org/1q4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q4t RCSB], [http://www.ebi.ac.uk/pdbsum/1q4t PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 27: | Line 27: | ||
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 1q4t" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 35: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: 4-hydroxybenzoyl-CoA thioesterase]] | [[Category: 4-hydroxybenzoyl-CoA thioesterase]] | ||
[[Category: Arthrobacter sp]] | [[Category: Arthrobacter sp. dsm20407]] | ||
[[Category: Dunaway-Mariano, D]] | [[Category: Dunaway-Mariano, D]] | ||
[[Category: Holden, H M]] | [[Category: Holden, H M]] | ||
Revision as of 16:21, 11 September 2015
crystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoAcrystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains three enzymes: a ligase, a dehalogenase, and a thioesterase. Here we describe the high resolution x-ray crystallographic structure of the 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. The tetrameric enzyme is a dimer of dimers with each subunit adopting the so-called "hot dog fold" composed of six strands of anti-parallel beta-sheet flanked on one side by a rather long alpha-helix. The dimers come together to form the tetramer with their alpha-helices facing outwards. This quaternary structure is in sharp contrast to that previously observed for the 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas species strain CBS-3, whereby the dimers forming the tetramer pack with their alpha-helices projecting toward the interfacial region. In the Arthrobacter thioesterase, each of the four active sites is formed by three of the subunits of the tetramer. On the basis of both structural and kinetic data, it appears that Glu73 is the active site base in the Arthrobacter thioesterase. Remarkably, this residue is located on the opposite side of the substrate-binding pocket compared with that observed for the Pseudomonas enzyme. Although these two bacterial thioesterases demonstrate equivalent catalytic efficiencies, substrate specificities, and metabolic functions, their quaternary structures, CoA-binding sites, and catalytic platforms are decidedly different. The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU.,Thoden JB, Zhuang Z, Dunaway-Mariano D, Holden HM J Biol Chem. 2003 Oct 31;278(44):43709-16. Epub 2003 Aug 7. PMID:12907670[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||