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6hli

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Revision as of 11:19, 29 July 2020

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

Structural highlights

6hli is a 4 chain structure with sequence from Aquae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	6hl2, 6hl3, 6hl4, 6hla
Gene:	nuoE, aq_574 (AQUAE), nuoF, aq_573 (AQUAE)
Activity:	NADH dehydrogenase (quinone), with EC number 1.6.5.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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). [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).

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schulte M, Frick K, Gnandt E, Jurkovic S, Burschel S, Labatzke R, Aierstock K, Fiegen D, Wohlwend D, Gerhardt S, Einsle O, Friedrich T. A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I. Nat Commun. 2019 Jun 11;10(1):2551. doi: 10.1038/s41467-019-10429-0. PMID:31186428 doi:http://dx.doi.org/10.1038/s41467-019-10429-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6hli"

@@ Line 3: / Line 3: @@
 <StructureSection load='6hli' size='340' side='right'caption='[[6hli]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6hli]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HLI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HLI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6hli]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HLI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6HLI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hl2|6hl2]], [[6hl3|6hl3]], [[6hl4|6hl4]], [[6hla|6hla]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nuoE, aq_574 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE]), nuoF, aq_573 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</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_(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>
-<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=6hli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hli OCA], [http://pdbe.org/6hli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hli RCSB], [http://www.ebi.ac.uk/pdbsum/6hli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hli ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6hli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hli OCA], [http://pdbe.org/6hli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hli RCSB], [http://www.ebi.ac.uk/pdbsum/6hli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hli ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 21: @@
 </div>
 <div class="pdbe-citations 6hli" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[NADH-quinone oxidoreductase|NADH-quinone oxidoreductase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Aquae]]
 [[Category: Large Structures]]
 [[Category: Einsle, O]]

6hli

From Proteopedia

Revision as of 11:19, 29 July 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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