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New page: left|200px<br /><applet load="1bvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvq, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...
 
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[[Image:1bvq.gif|left|200px]]<br /><applet load="1bvq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bvq, resolution 2.0&Aring;" />
'''THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.'''<br />


==Overview==
==THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.==
The soil-dwelling microbe, Pseudomonas sp. strain CBS-3, has attracted, recent attention due to its ability to survive on 4-chlorobenzoate as its, sole carbon source. The biochemical pathway by which this organism, converts 4-chlorobenzoate to 4-hydroxybenzoate consists of three enzymes:, 4-chlorobenzoyl-CoA ligase, 4-chlorobenzoyl-CoA dehalogenase, and, 4-hydroxybenzoyl-CoA thioesterase. Here we describe the three-dimensional, structure of the thioesterase determined to 2.0-A resolution. Each subunit, of the homotetramer is characterized by a five-stranded anti-parallel, beta-sheet and three major alpha-helices. While previous amino acid, sequence analyses failed to reveal any similarity between this, thioesterase and other known proteins, the results from this study clearly, demonstrate that the molecular architecture of 4-hydroxybenzoyl-CoA, thioesterase is topologically equivalent to that observed for, beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. On the, basis of the structural similarity between these two enzymes, the active, site of the thioesterase has been identified and a catalytic mechanism, proposed.
<StructureSection load='1bvq' size='340' side='right'caption='[[1bvq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._CBS3 Pseudomonas sp. CBS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvq OCA], [https://pdbe.org/1bvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvq RCSB], [https://www.ebi.ac.uk/pdbsum/1bvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/4HBT_PSEUC 4HBT_PSEUC] Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-CoA.<ref>PMID:1610806</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bvq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1bvq ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with EPE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/4-chlorobenzoate_dehalogenase 4-chlorobenzoate dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.6 3.8.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BVQ OCA].
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 
== References ==
==Reference==
<references/>
The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3., Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D, Holden HM, J Biol Chem. 1998 Dec 11;273(50):33572-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9837940 9837940]
__TOC__
[[Category: 4-chlorobenzoate dehalogenase]]
</StructureSection>
[[Category: Pseudomonas sp.]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Pseudomonas sp. CBS3]]
[[Category: Benning, M.M.]]
[[Category: Benning MM]]
[[Category: Dunaway-Mariano, D.]]
[[Category: Dunaway-Mariano D]]
[[Category: Holden, H.M.]]
[[Category: Holden HM]]
[[Category: EPE]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:57:26 2007''

Latest revision as of 06:39, 7 February 2024

THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.

1bvq, resolution 2.00Å

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