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New page: left|200px<br /><applet load="1iyz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iyz, resolution 2.80Å" /> '''Crystal Structures o...
 
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[[Image:1iyz.gif|left|200px]]<br /><applet load="1iyz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iyz, resolution 2.80&Aring;" />
'''Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH'''<br />


==Overview==
==Crystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH==
The crystal structures of the zeta-crystalline-like soluble quinone, oxidoreductase from Thermus thermophilus HB8 (QOR(Tt)) and of its complex, with NADPH have been determined at 2.3- and 2.8-A resolutions, respectively. QOR(Tt) is composed of two domains, and its overall fold is, similar to the folds of Escherichia coli quinone oxidoreductase (QOR(Ec)), and horse liver alcohol dehydrogenase. QOR(Tt) forms a homodimer in the, crystal by interaction of the betaF-strands in domain II, forming a large, beta-sheet that crosses the dimer interface. High thermostability of, QOR(Tt) was evidenced by circular dichroic measurement. NADPH is located, between the two domains in the QOR(Tt)-NADPH complex. The disordered, segment involved in the coenzyme binding of apo-QOR(Tt) becomes ordered, upon NADPH binding. The segment covers an NADPH-binding cleft and may, serve as a lid. The 2'-phosphate group of the adenine of NADPH is, surrounded by polar and positively charged residues in QOR(Tt), suggesting, that QOR(Tt) binds NADPH more readily than NADH. The putative, substrate-binding site of QOR(Tt), unlike that of QOR(Ec), is largely, blocked by nearby residues, permitting access only to small substrates., This may explain why QOR(Tt) has weak p-benzoquinone reduction activity, and is inactive with such large substrates of QOR(Ec) as, 5-hydroxy-1,4-naphthoquinone and phenanthraquinone.
<StructureSection load='1iyz' size='340' side='right'caption='[[1iyz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iyz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYZ 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=1iyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyz OCA], [https://pdbe.org/1iyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyz RCSB], [https://www.ebi.ac.uk/pdbsum/1iyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyz ProSAT], [https://www.topsan.org/Proteins/RSGI/1iyz TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8L3C8_THETH Q8L3C8_THETH]
== 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/iy/1iyz_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=1iyz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the zeta-crystalline-like soluble quinone oxidoreductase from Thermus thermophilus HB8 (QOR(Tt)) and of its complex with NADPH have been determined at 2.3- and 2.8-A resolutions, respectively. QOR(Tt) is composed of two domains, and its overall fold is similar to the folds of Escherichia coli quinone oxidoreductase (QOR(Ec)) and horse liver alcohol dehydrogenase. QOR(Tt) forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. High thermostability of QOR(Tt) was evidenced by circular dichroic measurement. NADPH is located between the two domains in the QOR(Tt)-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR(Tt) becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR(Tt), suggesting that QOR(Tt) binds NADPH more readily than NADH. The putative substrate-binding site of QOR(Tt), unlike that of QOR(Ec), is largely blocked by nearby residues, permitting access only to small substrates. This may explain why QOR(Tt) has weak p-benzoquinone reduction activity and is inactive with such large substrates of QOR(Ec) as 5-hydroxy-1,4-naphthoquinone and phenanthraquinone.


==About this Structure==
Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition.,Shimomura Y, Kakuta Y, Fukuyama K J Bacteriol. 2003 Jul;185(14):4211-8. PMID:12837796<ref>PMID:12837796</ref>
1IYZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with NDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NADPH:quinone_reductase NADPH:quinone reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.5 1.6.5.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IYZ OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: implication for NADPH and substrate recognition., Shimomura Y, Kakuta Y, Fukuyama K, J Bacteriol. 2003 Jul;185(14):4211-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837796 12837796]
</div>
[[Category: NADPH:quinone reductase]]
<div class="pdbe-citations 1iyz" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Fukuyama, K.]]
[[Category: Fukuyama K]]
[[Category: Kakuta, Y.]]
[[Category: Kakuta Y]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Shimomura Y]]
[[Category: Shimomura, Y.]]
[[Category: NDP]]
[[Category: protein-nadph complex]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomics]]
 
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