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| | <SX load='6gcs' size='340' side='right' viewer='molstar' caption='[[6gcs]], [[Resolution|resolution]] 4.32Å' scene=''> | | <SX load='6gcs' size='340' side='right' viewer='molstar' caption='[[6gcs]], [[Resolution|resolution]] 4.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gcs]] is a 42 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GCS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gcs]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Yarrowia_lipolytica Yarrowia lipolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GCS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZMP:S-[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]+TETRADECANETHIOATE'>ZMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.32Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZMP:S-[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]+TETRADECANETHIOATE'>ZMP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NADH_dehydrogenase NADH dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.3 1.6.99.3] </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=6gcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gcs OCA], [https://pdbe.org/6gcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gcs RCSB], [https://www.ebi.ac.uk/pdbsum/6gcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gcs 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=6gcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gcs OCA], [https://pdbe.org/6gcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gcs RCSB], [https://www.ebi.ac.uk/pdbsum/6gcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gcs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q9UUU2_YARLL Q9UUU2_YARLL]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain.[RuleBase:RU364066] [[https://www.uniprot.org/uniprot/A0A1D8NG21_YARLL A0A1D8NG21_YARLL]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [[https://www.uniprot.org/uniprot/NU6M_YARLI NU6M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/A0A1H6PXT9_YARLL A0A1H6PXT9_YARLL]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [[https://www.uniprot.org/uniprot/N7BM_YARLI N7BM_YARLI]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[UniProtKB:O97725] [[https://www.uniprot.org/uniprot/NU1M_YARLI NU1M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/NU5M_YARLI NU5M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/NU2M_YARLI NU2M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/NU4LM_YARLI NU4LM_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/NU4M_YARLI NU4M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/NU3M_YARLI NU3M_YARLI]] Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. [[https://www.uniprot.org/uniprot/Q6CGB4_YARLI Q6CGB4_YARLI]] Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.[PIRNR:PIRNR017016]
| + | [https://www.uniprot.org/uniprot/Q9UUU3_YARLL Q9UUU3_YARLL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: NADH dehydrogenase]] | |
| | [[Category: Yarrowia lipolytica]] | | [[Category: Yarrowia lipolytica]] |
| - | [[Category: Parey, K]] | + | [[Category: Parey K]] |
| - | [[Category: Vonck, J]] | + | [[Category: Vonck J]] |
| - | [[Category: Complex i]]
| + | |
| - | [[Category: Mitochondrion proton pumping]]
| + | |
| - | [[Category: Nadh dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ubiquinone]]
| + | |
| Structural highlights
Function
Q9UUU3_YARLL
Publication Abstract from PubMed
Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast Yarrowia lipolytica both in the deactive form and after capturing the enzyme during steady-state activity. The site of ubiquinone binding observed during turnover supports a two-state stabilization change mechanism for complex I.
Cryo-EM structure of respiratory complex I at work.,Parey K, Brandt U, Xie H, Mills DJ, Siegmund K, Vonck J, Kuhlbrandt W, Zickermann V Elife. 2018 Oct 2;7. pii: 39213. doi: 10.7554/eLife.39213. PMID:30277212[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Parey K, Brandt U, Xie H, Mills DJ, Siegmund K, Vonck J, Kuhlbrandt W, Zickermann V. Cryo-EM structure of respiratory complex I at work. Elife. 2018 Oct 2;7. pii: 39213. doi: 10.7554/eLife.39213. PMID:30277212 doi:http://dx.doi.org/10.7554/eLife.39213
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