1q4s

<table><tr><td colspan='2'>[[1q4s]] 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=1Q4S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Q4S FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1q4t|1q4t]], [[1q4u|1q4u]]</div></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=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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4s OCA], [http://pdbe.org/1q4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q4s RCSB], [http://www.ebi.ac.uk/pdbsum/1q4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q4s ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The 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<ref>PMID:12907670</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1q4s" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Arthrobacter sp. dsm20407]]

[[Category: Dunaway-Mariano, D]]

[[Category: Holden, H M]]

[[Category: Thoden, J B]]

[[Category: Zhuang, Z]]

[[Category: Thioesterase]]