- EMDB-4981: 3.6 Angstrom cryo-EM structure of the dimeric cytochrome b6f comp... -
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Entry
Database: EMDB / ID: EMD-4981
Title
3.6 Angstrom cryo-EM structure of the dimeric cytochrome b6f complex from Spinacia oleracea with natively bound thylakoid lipids and plastoquinone molecules
Map data
Sample
Complex: Spinach Cytochrome b6f complex with native bound plastoquinone and thylakoid lipids
Protein or peptide: x 8 types
Ligand: x 10 types
Keywords
Plastoquinol-plastocyanin oxido-reductase Cytochrome b6f Photosynthesis Electron transport / PHOTOSYNTHESIS
Function / homology
Function and homology information
cytochrome b6f complex / plastoquinol-plastocyanin reductase / plastoquinol--plastocyanin reductase activity / : / cytochrome complex assembly / photosynthetic electron transport chain / respiratory chain complex III / mitochondrial electron transport, ubiquinol to cytochrome c / : / chloroplast thylakoid membrane ...cytochrome b6f complex / plastoquinol-plastocyanin reductase / plastoquinol--plastocyanin reductase activity / : / cytochrome complex assembly / photosynthetic electron transport chain / respiratory chain complex III / mitochondrial electron transport, ubiquinol to cytochrome c / : / chloroplast thylakoid membrane / photosynthesis / proton transmembrane transport / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / oxidoreductase activity / iron ion binding / heme binding / mitochondrion / membrane / metal ion binding Similarity search - Function
Biotechnology and Biological Sciences Research Council
BB/M000265/1
United Kingdom
Biotechnology and Biological Sciences Research Council
BB/P002005/1
United Kingdom
Leverhulme Trust
RPG-2016-161
United Kingdom
Citation
Journal: Nature / Year: 2019 Title: Cryo-EM structure of the spinach cytochrome bf complex at 3.6 Å resolution. Authors: Lorna A Malone / Pu Qian / Guy E Mayneord / Andrew Hitchcock / David A Farmer / Rebecca F Thompson / David J K Swainsbury / Neil A Ranson / C Neil Hunter / Matthew P Johnson / Abstract: The cytochrome b f (cytb f ) complex has a central role in oxygenic photosynthesis, linking electron transfer between photosystems I and II and converting solar energy into a transmembrane ...The cytochrome b f (cytb f ) complex has a central role in oxygenic photosynthesis, linking electron transfer between photosystems I and II and converting solar energy into a transmembrane proton gradient for ATP synthesis. Electron transfer within cytb f occurs via the quinol (Q) cycle, which catalyses the oxidation of plastoquinol (PQH) and the reduction of both plastocyanin (PC) and plastoquinone (PQ) at two separate sites via electron bifurcation. In higher plants, cytb f also acts as a redox-sensing hub, pivotal to the regulation of light harvesting and cyclic electron transfer that protect against metabolic and environmental stresses. Here we present a 3.6 Å resolution cryo-electron microscopy (cryo-EM) structure of the dimeric cytb f complex from spinach, which reveals the structural basis for operation of the Q cycle and its redox-sensing function. The complex contains up to three natively bound PQ molecules. The first, PQ1, is located in one cytb f monomer near the PQ oxidation site (Q) adjacent to haem b and chlorophyll a. Two conformations of the chlorophyll a phytyl tail were resolved, one that prevents access to the Q site and another that permits it, supporting a gating function for the chlorophyll a involved in redox sensing. PQ2 straddles the intermonomer cavity, partially obstructing the PQ reduction site (Q) on the PQ1 side and committing the electron transfer network to turnover at the occupied Q site in the neighbouring monomer. A conformational switch involving the haem c propionate promotes two-electron, two-proton reduction at the Q site and avoids formation of the reactive intermediate semiquinone. The location of a tentatively assigned third PQ molecule is consistent with a transition between the Q and Q sites in opposite monomers during the Q cycle. The spinach cytb f structure therefore provides new insights into how the complex fulfils its catalytic and regulatory roles in photosynthesis.
History
Deposition
May 15, 2019
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Header (metadata) release
Jul 24, 2019
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Map release
Nov 13, 2019
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Update
Apr 9, 2025
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Current status
Apr 9, 2025
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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