1pjh

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{{Seed}}
 
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[[Image:1pjh.png|left|200px]]
 
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==Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily==
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The line below this paragraph, containing "STRUCTURE_1pjh", creates the "Structure Box" on the page.
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<StructureSection load='1pjh' size='340' side='right'caption='[[1pjh]], [[Resolution|resolution]] 2.10&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'>[[1pjh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PJH 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]] 2.1&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1pjh| PDB=1pjh | 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=1pjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pjh OCA], [https://pdbe.org/1pjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pjh RCSB], [https://www.ebi.ac.uk/pdbsum/1pjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pjh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECI1_YEAST ECI1_YEAST] Essential for the beta oxidation of unsaturated fatty acids.<ref>PMID:9837886</ref>
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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/pj/1pjh_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=1pjh 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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Subunits of the enzymes in the crotonase superfamily form tight trimeric disks. In most members of this protein superfamily these disks assemble further into hexamers. Here we report on the 2.1 A structure of a tight hexameric crystal form of the yeast peroxisomal delta(3)-delta(2)-enoyl-CoA isomerase (Eci1p). A comparison of this structure to a previously solved crystal form of Eci1p and other structures of this superfamily shows that there is much variability with respect to the relative distance between the disks and their relative orientations. In particular helices H2 and H9 are involved in the inter-trimer contacts and there are considerable structural differences in these helices in this superfamily. Helices H2 and H9 are near the catalytic cavity and it is postulated that the observed structural variability of these helices, stabilized by the different modes of assembly, has allowed the evolution of the wide range of substrate and catalytic specificity within this enzyme superfamily.
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===Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily===
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Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily.,Mursula AM, Hiltunen JK, Wierenga RK FEBS Lett. 2004 Jan 16;557(1-3):81-7. PMID:14741345<ref>PMID:14741345</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14741345}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1pjh" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14741345 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14741345}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1PJH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PJH OCA].
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==Reference==
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Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily., Mursula AM, Hiltunen JK, Wierenga RK, FEBS Lett. 2004 Jan 16;557(1-3):81-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14741345 14741345]
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[[Category: Dodecenoyl-CoA isomerase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Hiltunen JK]]
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[[Category: Hiltunen, J K.]]
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[[Category: Mursula AM]]
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[[Category: Mursula, A M.]]
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[[Category: Wierenga RK]]
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[[Category: Wierenga, R K.]]
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[[Category: Beta-beta-alpha spiral fold]]
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[[Category: Inter-trimer contact]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:10:45 2008''
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Current revision

Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily

PDB ID 1pjh

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