6hl3

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<StructureSection load='6hl3' size='340' side='right'caption='[[6hl3]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
<StructureSection load='6hl3' size='340' side='right'caption='[[6hl3]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6hl3]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HL3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6hl3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HL3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.04&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hl2|6hl2]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADH_dehydrogenase_(quinone) NADH dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.11 1.6.5.11] </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=6hl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hl3 OCA], [https://pdbe.org/6hl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hl3 RCSB], [https://www.ebi.ac.uk/pdbsum/6hl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hl3 ProSAT]</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=6hl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hl3 OCA], [http://pdbe.org/6hl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hl3 RCSB], [http://www.ebi.ac.uk/pdbsum/6hl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hl3 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NUOE_AQUAE NUOE_AQUAE]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). [[http://www.uniprot.org/uniprot/NUOF_AQUAE NUOF_AQUAE]] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
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[https://www.uniprot.org/uniprot/NUOE_AQUAE NUOE_AQUAE] NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 A resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by the reduction state of the nearby [Fe-S] cluster N1a. Fixation of the peptide bond by site-directed mutagenesis led to an inactivation of electron transfer and a decreased reactive oxygen species (ROS) production. We suggest the redox-gated peptide flip to represent a previously unrecognized molecular switch synchronizing NADH oxidation in response to the redox state of the complex as part of an intramolecular feed-back mechanism to prevent ROS production.
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A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.,Schulte M, Frick K, Gnandt E, Jurkovic S, Burschel S, Labatzke R, Aierstock K, Fiegen D, Wohlwend D, Gerhardt S, Einsle O, Friedrich T Nat Commun. 2019 Jun 11;10(1):2551. doi: 10.1038/s41467-019-10429-0. PMID:31186428<ref>PMID:31186428</ref>
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==See Also==
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*[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]]
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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 6hl3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aquifex aeolicus]]
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[[Category: Aquifex aeolicus VF5]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Einsle, O]]
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[[Category: Einsle O]]
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[[Category: Fiegen, D]]
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[[Category: Fiegen D]]
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[[Category: Friedrich, T]]
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[[Category: Friedrich T]]
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[[Category: Gerhardt, S]]
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[[Category: Gerhardt S]]
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[[Category: Gnandt, E]]
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[[Category: Gnandt E]]
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[[Category: Schulte, M]]
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[[Category: Schulte M]]
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[[Category: Aquifex aeolicus]]
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[[Category: Complex i]]
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[[Category: Electron transfer]]
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[[Category: Electron transport]]
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[[Category: Nuoef]]
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Current revision

wild-type NuoEF from Aquifex aeolicus - oxidized form bound to NAD+

PDB ID 6hl3

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