Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

Giraud, Marie‐France; Paumard, Patrick; Sanchez, Corinne; Brèthes, Daniel; Velours, Jean; Dautant, Alain

doi:10.1016/j.jsb.2011.10.015

Cited by 28 publications

(16 citation statements)

References 47 publications

(60 reference statements)

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“…Importantly, the addition of Mg.ATP substrate does not increase either the range of the flexion or the proportion of particles that are flexed. Instead, it limits the flexibility to a maximum of 10° (Figure 2B, Figure 4B, Movies S1-S3, S5), the angle that is most consistent with the proposed radial bending and observed variations in crystal structures of the subunit E/G heterodimer [26,31]. This more subtle movement (shown in Figure 2B, C and Movies S1-S3) is also consistent with the predicted flexibility within the V-ATPase [31].…”

Section: Discussionsupporting

confidence: 77%

“…This wobble has to be accommodated by radial movement of the stator filament. Flexibility within F-ATPase is also suggested by crystallographic studies of F 1 - c 10 complexes [26,27] where the central axle pivots at its point of contact with the c -ring, such that axle and c -ring are no longer co-axial as required for smooth power transmission. Although the ~11° flexion observed in these studies is imposed by crystal lattice interactions and likely also to be influenced by the absence of the membrane-anchored part of the stator, subunit- a , it is reasonable to suppose that it does report on natural flexibility.…”

Section: Discussionmentioning

confidence: 99%

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Flexibility within the Rotor and Stators of the Vacuolar H+-ATPase

et al. 2013

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The V-ATPase is a membrane-bound protein complex which pumps protons across the membrane to generate a large proton motive force through the coupling of an ATP-driven 3-stroke rotary motor (V1) to a multistroke proton pump (Vo). This is done with near 100% efficiency, which is achieved in part by flexibility within the central rotor axle and stator connections, allowing the system to flex to minimise the free energy loss of conformational changes during catalysis. We have used electron microscopy to reveal distinctive bending along the V-ATPase complex, leading to angular displacement of the V1 domain relative to the Vo domain to a maximum of ~30°. This has been complemented by elastic network normal mode analysis that shows both flexing and twisting with the compliance being located in the rotor axle, stator filaments, or both. This study provides direct evidence of flexibility within the V-ATPase and by implication in related rotary ATPases, a feature predicted to be important for regulation and their high energetic efficiencies.

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Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Flexibility within the Rotor and Stators of the Vacuolar H+-ATPase

et al. 2013

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“…At the end of the N-terminal helix, Asn40 forms a sharp turn leading into another short 3 10 helix (residues 41–43) that precedes the C-terminal transmembrane span. Together with Arg39, Pro41, and Ser42, these form a highly conserved region, which apparently form an interaction motif with subunits γ, δ, and ε of the central stalk of the F 1 complex 4,6,29,30 . Consequently, the N- and C-termini are located in the intermembrane mitochondrial space.…”

Section: Resultsmentioning

confidence: 99%

Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation

Symerský

Pagadala

Osowski

et al. 2012

Nat Struct Mol Biol

116

137

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The proton pores of F1Fo-ATP synthases consist of a ring of c-subunits, which rotates driven by downhill proton diffusion. An essential carboxylate side chain in the c-subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are presented of the c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologues, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c-subunit, which facilitates proton loading and release.

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“…The catalytic (αβ) 3 hexamer is held stationary relative to the membrane region by the peripheral stalk (10,11). Several high-resolution structures of the F 1 /rotor ring complexes have been solved by X-ray crystallography (12)(13)(14)(15)(16), and the structure of the complete assembly has been determined by cryoelectron microscopy (cryo-EM) (10,(17)(18)(19)(20).…”

mentioning

confidence: 99%

Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria

Muhleip

Joos

Wigge

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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F 1 F o -ATP synthases are universal energy-converting membrane protein complexes that synthesize ATP from ADP and inorganic phosphate. In mitochondria of yeast and mammals, the ATP synthase forms V-shaped dimers, which assemble into rows along the highly curved ridges of lamellar cristae. Using electron cryotomography and subtomogram averaging, we have determined the in situ structure and organization of the mitochondrial ATP synthase dimer of the ciliate Paramecium tetraurelia. The ATP synthase forms U-shaped dimers with parallel monomers. Each complex has a prominent intracrista domain, which links the c-ring of one monomer to the peripheral stalk of the other. Close interaction of intracrista domains in adjacent dimers results in the formation of helical ATP synthase dimer arrays, which differ from the loose dimer rows in all other organisms observed so far. The parameters of the helical arrays match those of the cristae tubes, suggesting the unique features of the P. tetraurelia ATP synthase are directly responsible for generating the helical tubular cristae. We conclude that despite major structural differences between ATP synthase dimers of ciliates and other eukaryotes, the formation of ATP synthase dimer rows is a universal feature of mitochondria and a fundamental determinant of cristae morphology.cryoelectron microscopy | subtomogram averaging | Paramecium | macromolecular organization | serial block face imaging F 1 F o -ATP synthases are ubiquitous, highly conserved energyconverting membrane protein complexes. ATP synthases produce ATP from ADP and inorganic phosphate (P i ) by rotary catalysis (1, 2) using the energy stored in a transmembrane electrochemical gradient. The ∼600-kDa monomer of the mitochondrial ATP synthase is composed of a soluble F 1 subcomplex and a membranebound F o subcomplex (3). The main components of the F 1 subcomplex are the (αβ) 3 hexamer and the central stalk (4). The F o subcomplex includes a rotor ring of 8-15 hydrophobic c subunits (5), the peripheral stalk, and several small hydrophobic stator subunits. Protons flowing through the membrane part of the F o subcomplex drive the rotation of the c-ring (6-9). The central stalk transmits the torque generated by c-ring rotation to the catalytic head of the F 1 subcomplex, where it induces conformational changes of the α and β subunits that result in phosphate bond formation and the generation of ATP. The catalytic (αβ) 3 hexamer is held stationary relative to the membrane region by the peripheral stalk (10, 11). Several high-resolution structures of the F 1 /rotor ring complexes have been solved by X-ray crystallography (12-16), and the structure of the complete assembly has been determined by cryoelectron microscopy (cryo-EM) (10,(17)(18)(19)(20).In mitochondria, the ATP synthase forms dimers in the inner membrane. In fungi, plants, and metazoans, the dimers are V-shaped and associate into rows along the highly curved ridges of lamellar cristae (19)(20)(21)(22). F o subcomplexes of the two monomers in the dimer interact in...

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Rotor architecture in the yeast and bovine F1-c-ring complexes of F-ATP synthase

Cited by 28 publications

References 47 publications

Flexibility within the Rotor and Stators of the Vacuolar H+-ATPase

Flexibility within the Rotor and Stators of the Vacuolar H+-ATPase

Structure of the c10 ring of the yeast mitochondrial ATP synthase in the open conformation

Helical arrays of U-shaped ATP synthase dimers form tubular cristae in ciliate mitochondria

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