8ab9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ab9]] is a 20 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=8AB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AB9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ab9]] is a 20 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=8AB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AB9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=XP4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE'>XP4</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]] 3.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene>, <scene name='pdbligand=XP4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE'>XP4</scene></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=8ab9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ab9 OCA], [https://pdbe.org/8ab9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ab9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ab9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ab9 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=8ab9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ab9 OCA], [https://pdbe.org/8ab9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ab9 RCSB], [https://www.ebi.ac.uk/pdbsum/8ab9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ab9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
Movement of the Rieske domain of the iron-sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII(2) from Yarrowia lipolytica at resolutions up to 2.0 A under different conditions, with different redox states of the cofactors of the high-potential chain. All possible permutations of three primary positions were observed, indicating that the two halves of the dimeric complex act independently. Addition of the substrate analogue decylubiquinone to CIII(2) with a reduced high-potential chain increased the occupancy of the Q(o) site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c(1) subunits varied depending on the redox state and substrate. In the absence of quinols, the reduced Rieske domain interacted more closely with cytochrome b and cytochrome c(1) than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd(1)-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain. | |||
Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III(2) by cryo-EM.,Wieferig JP, Kuhlbrandt W IUCrJ. 2023 Jan 1;10(Pt 1):27-37. doi: 10.1107/S2052252522010570. PMID:36598500<ref>PMID:36598500</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8ab9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Yarrowia lipolytica]] | [[Category: Yarrowia lipolytica]] | ||
[[Category: | [[Category: Kuhlbrandt W]] | ||
[[Category: Wieferig | [[Category: Wieferig JP]] | ||
Latest revision as of 12:45, 9 October 2024
Complex III2 from Yarrowia lipolytica, ascorbate-reduced, b-positionComplex III2 from Yarrowia lipolytica, ascorbate-reduced, b-position
Structural highlights
Publication Abstract from PubMedMovement of the Rieske domain of the iron-sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII(2) from Yarrowia lipolytica at resolutions up to 2.0 A under different conditions, with different redox states of the cofactors of the high-potential chain. All possible permutations of three primary positions were observed, indicating that the two halves of the dimeric complex act independently. Addition of the substrate analogue decylubiquinone to CIII(2) with a reduced high-potential chain increased the occupancy of the Q(o) site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c(1) subunits varied depending on the redox state and substrate. In the absence of quinols, the reduced Rieske domain interacted more closely with cytochrome b and cytochrome c(1) than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd(1)-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain. Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III(2) by cryo-EM.,Wieferig JP, Kuhlbrandt W IUCrJ. 2023 Jan 1;10(Pt 1):27-37. doi: 10.1107/S2052252522010570. PMID:36598500[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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