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New page: left|200px<br /><applet load="1ehk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ehk, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1ehk.gif|left|200px]]<br /><applet load="1ehk" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ehk, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE ABERRANT BA3-CYTOCHROME-C OXIDASE FROM THERMUS THERMOPHILUS==
Cytochrome c oxidase is a respiratory enzyme catalysing the, energy-conserving reduction of molecular oxygen to water. The crystal, structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has, been determined to 2.4 A resolution using multiple anomalous dispersion, (MAD) phasing and led to the discovery of a novel subunit IIa. A, structure-based sequence alignment of this phylogenetically very distant, oxidase with the other structurally known cytochrome oxidases leads to the, identification of sequence motifs and residues that seem to be, indispensable for the function of the haem copper oxidases, e.g. a new, electron transfer pathway leading directly from Cu(A) to Cu(B). Specific, features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen, atom (O(2-), OH(-) or H(2)O) as bridging ligand at the active site and the, mainly hydrophobic character of the interactions that stabilize the, electron transfer complex between this oxidase and its substrate, cytochrome c. New aspects of the proton pumping mechanism could be, identified.
<StructureSection load='1ehk' size='340' side='right'caption='[[1ehk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ehk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHK 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1ehk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehk OCA], [https://pdbe.org/1ehk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehk RCSB], [https://www.ebi.ac.uk/pdbsum/1ehk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COX1_THET8 COX1_THET8]
== 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/eh/1ehk_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=1ehk ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytochrome c oxidase is a respiratory enzyme catalysing the energy-conserving reduction of molecular oxygen to water. The crystal structure of the ba(3)-cytochrome c oxidase from Thermus thermophilus has been determined to 2.4 A resolution using multiple anomalous dispersion (MAD) phasing and led to the discovery of a novel subunit IIa. A structure-based sequence alignment of this phylogenetically very distant oxidase with the other structurally known cytochrome oxidases leads to the identification of sequence motifs and residues that seem to be indispensable for the function of the haem copper oxidases, e.g. a new electron transfer pathway leading directly from Cu(A) to Cu(B). Specific features of the ba(3)-oxidase include an extended oxygen input channel, which leads directly to the active site, the presence of only one oxygen atom (O(2-), OH(-) or H(2)O) as bridging ligand at the active site and the mainly hydrophobic character of the interactions that stabilize the electron transfer complex between this oxidase and its substrate cytochrome c. New aspects of the proton pumping mechanism could be identified.


==About this Structure==
Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus.,Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME EMBO J. 2000 Apr 17;19(8):1766-76. PMID:10775261<ref>PMID:10775261</ref>
1EHK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with BNG, CU, HEM, HAS and CUA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EHK OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus., Soulimane T, Buse G, Bourenkov GP, Bartunik HD, Huber R, Than ME, EMBO J. 2000 Apr 17;19(8):1766-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10775261 10775261]
</div>
[[Category: Cytochrome-c oxidase]]
<div class="pdbe-citations 1ehk" style="background-color:#fffaf0;"></div>
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Bartunik, H.D.]]
[[Category: Bourenkov, G.P.]]
[[Category: Buse, G.]]
[[Category: Huber, R.]]
[[Category: Soulimane, T.]]
[[Category: Than, M.E.]]
[[Category: BNG]]
[[Category: CU]]
[[Category: CUA]]
[[Category: HAS]]
[[Category: HEM]]
[[Category: cytochrome-c oxidase]]
[[Category: membrane protein]]
[[Category: thermus thermophilus]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:00:39 2007''
==See Also==
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Bartunik HD]]
[[Category: Bourenkov GP]]
[[Category: Buse G]]
[[Category: Huber R]]
[[Category: Soulimane T]]
[[Category: Than ME]]
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