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3m9c

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3m9c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9C FirstGlance]. <br>
<table><tr><td colspan='2'>[[3m9c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9C FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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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]] 3.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m9s|3m9s]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </span></td></tr>
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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=3m9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9c OCA], [https://pdbe.org/3m9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9c RCSB], [https://www.ebi.ac.uk/pdbsum/3m9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9c ProSAT]</span></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=3m9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9c OCA], [https://pdbe.org/3m9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9c RCSB], [https://www.ebi.ac.uk/pdbsum/3m9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9c ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Complex I is the first enzyme of the respiratory chain and has a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation by an unknown mechanism. Dysfunction of complex I has been implicated in many human neurodegenerative diseases. We have determined the structure of its hydrophilic domain previously. Here, we report the alpha-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 A resolution. The antiporter-like subunits NuoL/M/N each contain 14 conserved transmembrane (TM) helices. Two of them are discontinuous, as in some transporters. Unexpectedly, subunit NuoL also contains a 110-A long amphipathic alpha-helix, spanning almost the entire length of the domain. Furthermore, we have determined the structure of the entire complex I from Thermus thermophilus at 4.5 A resolution. The L-shaped assembly consists of the alpha-helical model for the membrane domain, with 63 TM helices, and the known structure of the hydrophilic domain. The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic alpha-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation.
 
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The architecture of respiratory complex I.,Efremov RG, Baradaran R, Sazanov LA Nature. 2010 May 27;465(7297):441-5. PMID:20505720<ref>PMID:20505720</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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<div class="pdbe-citations 3m9c" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]]
*[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baradaran, R]]
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[[Category: Baradaran R]]
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[[Category: Efremov, R G]]
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[[Category: Efremov RG]]
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[[Category: Sazanov, L A]]
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[[Category: Sazanov LA]]
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[[Category: Complex i]]
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[[Category: Electron transport]]
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[[Category: Membrane protein]]
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[[Category: Oxidoreductase]]
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[[Category: Respiratory chain]]
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Current revision

Crystal structure of the membrane domain of respiratory complex I from Escherichia coli

PDB ID 3m9c

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