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[[Image:1e7p.gif|left|200px]]<br /><applet load="1e7p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1e7p, resolution 3.10&Aring;" />
'''QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''<br />


==Overview==
==QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES==
Quinol:fumarate reductase (QFR) is a membrane protein complex that couples, the reduction of fumarate to succinate to the oxidation of quinol to, quinone. Previously, the crystal structure of QFR from Wolinella, succinogenes was determined based on two different crystal forms, and the, site of fumarate binding in the flavoprotein subunit A of the enzyme was, located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., &amp; Michel, H. (1999) Nature 402, 377--385]., Here we describe the structure of W. succinogenes QFR based on a third, crystal form and refined at 3.1 A resolution. Compared with the previous, crystal forms, the capping domain is rotated in this structure by, approximately 14 degrees relative to the FAD-binding domain. As a, consequence, the topology of the dicarboxylate binding site is much more, similar to those of membrane-bound and soluble fumarate reductase enzymes, from other organisms than to that found in the previous crystal forms of, W. succinogenes QFR. This and the effects of the replacement of Arg A301, by Glu or Lys by site-directed mutagenesis strongly support a common, mechanism for fumarate reduction in this superfamily of enzymes.
<StructureSection load='1e7p' size='340' side='right'caption='[[1e7p]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1e7p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7P 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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1e7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7p OCA], [https://pdbe.org/1e7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7p RCSB], [https://www.ebi.ac.uk/pdbsum/1e7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
== 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/e7/1e7p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1e7p ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Quinol:fumarate reductase (QFR) is a membrane protein complex that couples the reduction of fumarate to succinate to the oxidation of quinol to quinone. Previously, the crystal structure of QFR from Wolinella succinogenes was determined based on two different crystal forms, and the site of fumarate binding in the flavoprotein subunit A of the enzyme was located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kroger, A., Auer, M., &amp; Michel, H. (1999) Nature 402, 377--385]. Here we describe the structure of W. succinogenes QFR based on a third crystal form and refined at 3.1 A resolution. Compared with the previous crystal forms, the capping domain is rotated in this structure by approximately 14 degrees relative to the FAD-binding domain. As a consequence, the topology of the dicarboxylate binding site is much more similar to those of membrane-bound and soluble fumarate reductase enzymes from other organisms than to that found in the previous crystal forms of W. succinogenes QFR. This and the effects of the replacement of Arg A301 by Glu or Lys by site-directed mutagenesis strongly support a common mechanism for fumarate reduction in this superfamily of enzymes.


==About this Structure==
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction.,Lancaster CR, Gross R, Simon J Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:11248702<ref>PMID:11248702</ref>
1E7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes] with NA, HEM, FES, F3S, SF4, FAD, MLA and LMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] Known structural/functional Sites: <scene name='pdbsite=FA1:Fad Covalent Bond To Protein For Chain A'>FA1</scene>, <scene name='pdbsite=FA2:Fad Covalent Bond To Protein For Chain D'>FA2</scene>, <scene name='pdbsite=FA3:Fad Covalent Bond To Protein For Chain G'>FA3</scene>, <scene name='pdbsite=FA4:Fad Covalent Bond To Protein For Chain K'>FA4</scene>, <scene name='pdbsite=FS1:Fe4s4 Fe Sulphur Centre Ligands For Chain B'>FS1</scene>, <scene name='pdbsite=FS2:Fe4s4 Fe Sulphur Centre Ligands For Chain E'>FS2</scene>, <scene name='pdbsite=FS3:Fe2s2 Fe Sulphur Centre Ligands For Chain B'>FS3</scene>, <scene name='pdbsite=FS4:Fe2s2 Fe Sulphur Centre Ligands For Chain E'>FS4</scene>, <scene name='pdbsite=FS5:Fe3s4 Fe Sulphur Centre Ligands For Chain B'>FS5</scene>, <scene name='pdbsite=FS6:Fe3s4 Fe Sulphur Centre Ligands For Chain E'>FS6</scene>, <scene name='pdbsite=FS7:Fe4s4 Fe Sulphur Centre Ligands For Chain G'>FS7</scene>, <scene name='pdbsite=FS8:Fe4s4 Fe Sulphur Centre Ligands For Chain K'>FS8</scene>, <scene name='pdbsite=FS9:Fe2s2 Fe Sulphur Centre Ligands For Chain G'>FS9</scene>, <scene name='pdbsite=FSA:Fe2s2 Fe Sulphur Centre Ligands For Chain K'>FSA</scene>, <scene name='pdbsite=FSB:Fe3s4 Fe Sulphur Centre Ligands For Chain G'>FSB</scene>, <scene name='pdbsite=FSC:Fe3s4 Fe Sulphur Centre Ligands For Chain K'>FSC</scene>, <scene name='pdbsite=HE1:Haem Axial Ligands For Chain C'>HE1</scene>, <scene name='pdbsite=HE2:Haem Axial Ligands For Chain F'>HE2</scene>, <scene name='pdbsite=HE3:Haem Axial Ligands For Chain I'>HE3</scene> and <scene name='pdbsite=HE4:Haem Axial Ligands For Chain L'>HE4</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction., Lancaster CR, Gross R, Simon J, Eur J Biochem. 2001 Mar;268(6):1820-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11248702 11248702]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1e7p" style="background-color:#fffaf0;"></div>
[[Category: Succinate dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]
[[Category: Lancaster, C.R.D.]]
[[Category: Kroeger A]]
[[Category: F3S]]
[[Category: Lancaster CRD]]
[[Category: FAD]]
[[Category: FES]]
[[Category: HEM]]
[[Category: LMT]]
[[Category: MLA]]
[[Category: NA]]
[[Category: SF4]]
[[Category: citric acid cycle]]
[[Category: dihaem cytochrome b]]
[[Category: flavoprotein]]
[[Category: fumarate reductase]]
[[Category: iron-sulphur protein]]
[[Category: oxidoreductase]]
[[Category: respiratory chain]]
[[Category: succinate dehydrogenase]]
 
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