3m9c
From Proteopedia
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- | + | ==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=''> |
- | + | == 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> | ||
+ | </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> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9s|3m9s]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_dehydrogenase_(ubiquinone) NADH dehydrogenase (ubiquinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.3 1.6.5.3] </span></td></tr> | ||
+ | <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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | ||
- | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | + | </div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Baradaran, R | + | [[Category: Baradaran, R]] |
- | [[Category: Efremov, R G | + | [[Category: Efremov, R G]] |
- | [[Category: Sazanov, L A | + | [[Category: Sazanov, L A]] |
[[Category: Complex i]] | [[Category: Complex i]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] |
Revision as of 14:43, 18 December 2014
Crystal structure of the membrane domain of respiratory complex I from Escherichia coli
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