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6q9d

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Current revision

CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2

6q9d, resolution 3.80Å

Structural highlights

6q9d is a 18 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	6q9b
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[W5NQT7_SHEEP] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [W5QAH8_SHEEP] 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:PIRNR005822] [B9VGZ9_SHEEP] 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.[RuleBase:RU363103]

Publication Abstract from PubMed

The mitochondrial electron transport chain complexes are organized into supercomplexes (SCs) of defined stoichiometry, which have been proposed to regulate electron flux via substrate channeling. We demonstrate that CoQ trapping in the isolated SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure, resolved at up to 3.8 A in four distinct states, suggests that CoQ oxidation may be rate limiting because of unequal access of CoQ to the active sites of CIII2. CI shows a transition between "closed" and "open" conformations, accompanied by the striking rotation of a key transmembrane helix. Furthermore, the state of CI affects the conformational flexibility within CIII2, demonstrating crosstalk between the enzymes. CoQ was identified at only three of the four binding sites in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally relevant manner. Together, these observations indicate a more nuanced functional role for the SCs.

Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk.,Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA Mol Cell. 2019 Sep 19;75(6):1131-1146.e6. doi: 10.1016/j.molcel.2019.07.022. Epub, 2019 Sep 3. PMID:31492636^[1]

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

References

↑ Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of Respiratory Supercomplex I+III2 Reveal Functional and Conformational Crosstalk. Mol Cell. 2019 Sep 19;75(6):1131-1146.e6. doi: 10.1016/j.molcel.2019.07.022. Epub, 2019 Sep 3. PMID:31492636 doi:http://dx.doi.org/10.1016/j.molcel.2019.07.022

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6q9d"

@@ Line 1: / Line 1: @@
 ==CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2==
-<StructureSection load='6q9d' size='340' side='right'caption='[[6q9d]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<SX load='6q9d' size='340' side='right' viewer='molstar' caption='[[6q9d]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6q9d]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q9D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6q9d]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q9D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Q9D 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=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='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=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>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6q9b|6q9b]]</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=6q9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q9d OCA], [http://pdbe.org/6q9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q9d RCSB], [http://www.ebi.ac.uk/pdbsum/6q9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q9d 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=6q9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q9d OCA], [http://pdbe.org/6q9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q9d RCSB], [http://www.ebi.ac.uk/pdbsum/6q9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q9d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/W5NQT7_SHEEP W5NQT7_SHEEP]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [[http://www.uniprot.org/uniprot/B9VGZ9_SHEEP B9VGZ9_SHEEP]] 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.[RuleBase:RU363103] [[http://www.uniprot.org/uniprot/W5QAH8_SHEEP W5QAH8_SHEEP]] 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:PIRNR005822]
+[[http://www.uniprot.org/uniprot/W5NQT7_SHEEP W5NQT7_SHEEP]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722] [[http://www.uniprot.org/uniprot/W5QAH8_SHEEP W5QAH8_SHEEP]] 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:PIRNR005822] [[http://www.uniprot.org/uniprot/B9VGZ9_SHEEP B9VGZ9_SHEEP]] 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.[RuleBase:RU363103]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Large Structures]]
 [[Category: Ovis aries]]

6q9d

From Proteopedia

Current revision

CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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