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| ==Crystal structure of the membrane domain of respiratory complex I from Escherichia coli== | | ==Crystal structure of the membrane domain of respiratory complex I from Escherichia coli== |
| <StructureSection load='3m9c' size='340' side='right' caption='[[3m9c]], [[Resolution|resolution]] 3.90Å' scene=''> | | <StructureSection load='3m9c' size='340' side='right'caption='[[3m9c]], [[Resolution|resolution]] 3.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3m9c]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> |
| </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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9s|3m9s]]</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> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH:ubiquinone_reductase_(H(+)-translocating) NADH:ubiquinone reductase (H(+)-translocating)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m9c RCSB], [http://www.ebi.ac.uk/pdbsum/3m9c PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]] |
| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| [[Category: Baradaran, R]] | | [[Category: Large Structures]] |
| [[Category: Efremov, R G]] | | [[Category: Baradaran R]] |
| [[Category: Sazanov, L A]] | | [[Category: Efremov RG]] |
| [[Category: Complex i]] | | [[Category: Sazanov LA]] |
| [[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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