2et6: Difference between revisions

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OCA

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-[[Image:2et6.gif|left|200px]]<br /><applet load="2et6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2et6, resolution 2.22&Aring;" />
-'''(3R)-Hydroxyacyl-CoA Dehydrogenase Domain of Candida tropicalis Peroxisomal Multifunctional Enzyme Type 2'''<br />
-==Overview==
+==(3R)-Hydroxyacyl-CoA Dehydrogenase Domain of Candida tropicalis Peroxisomal Multifunctional Enzyme Type 2==
-(3R)-hydroxyacyl-CoA dehydrogenase is part of multifunctional enzyme type, 2 (MFE-2) of peroxisomal fatty acid beta-oxidation. The MFE-2 protein from, yeasts contains in the same polypeptide chain two dehydrogenases (A and, B), which possess difference in substrate specificity. The crystal, structure of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenase AB, heterodimer, consisting of dehydrogenase A and B, determined at the, resolution of 2.2A, shows overall similarity with the prototypic, counterpart from rat, but also important differences that explain the, substrate specificity differences observed. Docking studies suggest that, dehydrogenase A binds the hydrophobic fatty acyl chain of a, medium-chain-length ((3R)-OH-C10) substrate as bent into the binding, pocket, whereas the short-chain substrates are dislocated by two, mechanisms: (i) a short-chain-length 3-hydroxyacyl group ((3R)-OH-C4) does, not reach the hydrophobic contacts needed for anchoring the substrate into, the active site; and (ii) Leu44 in the loop above the NAD(+) cofactor, attracts short-chain-length substrates away from the active site., Dehydrogenase B, which can use a (3R)-OH-C4 substrate, has a more shallow, binding pocket and the substrate is correctly placed for catalysis. Based, on the current structure, and together with the structure of the, 2-enoyl-CoA hydratase 2 unit of yeast MFE-2 it becomes obvious that in, yeast and mammalian MFE-2s, despite basically identical functional, domains, the assembly of these domains into a mature, dimeric, multifunctional enzyme is very different.
+<StructureSection load='2et6' size='340' side='right'caption='[[2et6]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2et6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ET6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ET6 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]] 2.22&#8491;</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=2et6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2et6 OCA], [https://pdbe.org/2et6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2et6 RCSB], [https://www.ebi.ac.uk/pdbsum/2et6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2et6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FOX2_CANTR FOX2_CANTR] Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
+== 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/et/2et6_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=2et6 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-ET6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ET6 OCA].
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure of yeast peroxisomal multifunctional enzyme: structural basis for substrate specificity of (3R)-hydroxyacyl-CoA dehydrogenase units., Ylianttila MS, Pursiainen NV, Haapalainen AM, Juffer AH, Poirier Y, Hiltunen JK, Glumoff T, J Mol Biol. 2006 May 19;358(5):1286-95. Epub 2006 Mar 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16574148 16574148]
 [[Category: Candida tropicalis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Glumoff, T.]]
+[[Category: Glumoff T]]
-[[Category: Hiltunen, J.K.]]
+[[Category: Hiltunen JK]]
-[[Category: Ylianttila, M.S.]]
+[[Category: Ylianttila MS]]
-[[Category: beta-oxidation]]
-[[Category: dehydrogenase]]
-[[Category: mfe-2]]
-[[Category: oxidoreductase]]
-[[Category: peroxisome]]
-[[Category: sdr]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:07:41 2007''