1q4u

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[[Image:1q4u.jpg|left|200px]]
 
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==Crystal structure of 4-hydroxybenzoyl CoA thioesterase from arthrobacter sp. strain SU complexed with 4-hydroxybenzyl CoA==
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The line below this paragraph, containing "STRUCTURE_1q4u", creates the "Structure Box" on the page.
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<StructureSection load='1q4u' size='340' side='right'caption='[[1q4u]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1q4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_sp._SU Arthrobacter sp. SU]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q4U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CA:4-HYDROXYBENZYL+COENZYME+A'>4CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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{{STRUCTURE_1q4u| PDB=1q4u | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4u OCA], [https://pdbe.org/1q4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q4u RCSB], [https://www.ebi.ac.uk/pdbsum/1q4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q4u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/4HBT_ARTSP 4HBT_ARTSP]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q4/1q4u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1q4u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal structure of 4-hydroxybenzoyl CoA thioesterase from arthrobacter sp. strain SU complexed with 4-hydroxybenzyl CoA'''
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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>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1Q4U is a [[Single protein]] structure of 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=1Q4U OCA].
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</div>
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<div class="pdbe-citations 1q4u" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12907670 12907670]
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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[[Category: 4-hydroxybenzoyl-CoA thioesterase]]
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== References ==
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[[Category: Arthrobacter sp.]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Dunaway-Mariano, D.]]
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</StructureSection>
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[[Category: Holden, H M.]]
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[[Category: Arthrobacter sp. SU]]
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[[Category: Thoden, J B.]]
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[[Category: Large Structures]]
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[[Category: Zhuang, Z.]]
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[[Category: Dunaway-Mariano D]]
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[[Category: Hot-dog]]
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[[Category: Holden HM]]
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[[Category: Thioesterase]]
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[[Category: Thoden JB]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:52:02 2008''
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[[Category: Zhuang Z]]

Current revision

Crystal structure of 4-hydroxybenzoyl CoA thioesterase from arthrobacter sp. strain SU complexed with 4-hydroxybenzyl CoA

PDB ID 1q4u

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