Structure of the Rotor Ring of F-Type Na
            <sup>+</sup>
            -ATPase from
            <i>Ilyobacter tartaricus</i>

Meier, Thomas; Polzer, Patrick; Diederichs, Kay; Welte, Wolfram; Dimroth, Peter

doi:10.1126/science.1111199

Cited by 360 publications

(391 citation statements)

References 34 publications

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“…The rotation is biased to go in the required direction by the direction of the proton motive force across the membrane. Crystal structures of the proteolipid-ring complex from both V-and F-type ATPases show that the conserved protonatable residue of each monomer in the ring would be buried in a lipid bilayer with no direct accessibility of solvated protons to the residue (26,36). Therefore, in T. thermophilus, the I-subunit must contain both the periplasmic and the cytoplasmic half-channels that conduct protons to and from the Glu 63 residues of the ring.…”

mentioning

confidence: 99%

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

Lau

Rubinstein

2010

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

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The eubacterium Thermus thermophilus uses a macromolecular assembly closely related to eukaryotic V-ATPase to produce its supply of ATP. This simplified V-ATPase offers several advantages over eukaryotic V-ATPases for structural analysis and investigation of the mechanism of the enzyme. Here we report the structure of the complex at ∼16 Å resolution as determined by single particle electron cryomicroscopy (cryo-EM). The resolution of the map and our use of cryo-EM, rather than negative stain EM, reveals detailed information about the internal organization of the assembly. We could separate the map into segments corresponding to subunits A and B, the threefold pseudosymmetric C-subunit, a central rotor consisting of subunits D and F, the L-ring, the stator subcomplex consisting of subunits I, E, and G, and a micelle of bound detergent. The architecture of the V O region shows a remarkably small area of contact between the I-subunit and the ring of L-subunits and is consistent with a two half-channel model for proton translocation. The arrangement of structural elements in V O gives insight into the mechanism of torque generation from proton translocation. membrane protein | single particle analysis V acuolar-type ATPases (V-ATPases) in eukaryotes function as ATP-driven proton pumps that acidify intracellular compartments including lysosomes, endosomes, and secretory vesicles. This acidification, in turn, affects diverse processes including protein sorting and degradation, overall ion homeostasis, and protection of cells from oxidative stress (1). Extracellular acidification by V-ATPases is linked to tumor invasion and metastasis and osteoporosis (2). F-type ATP synthases and V-type ATPases are evolutionarily related but differ in the details of subunit composition and arrangement. Both F-and V-type ATPases use a rotary catalytic mechanism where proton translocation through the membranebound F O or V O region, respectively, generates a torque on a rotor subcomplex that drives ATP synthesis in the F 1 or V 1 region. The enzymes can also run in the opposite direction with ATP hydrolysis in the F 1 or V 1 region resulting in proton pumping through F O or V O . This mechanism has been the subject of a large body of research for F-type ATP synthases (e.g., 3-5), but there has also been direct demonstration of rotary catalysis for V-ATPases (6). Some archaea and eubacteria use a complex more closely related to VATPase than F-type ATP synthase, sometimes called an A-ATPase, to generate their supply of ATP (7).The V-ATPase from the eubacterium Thermus thermophilus is composed of nine different subunits with a stoichiometry of A 3 B 3 CDE 2 FG 2 IL 12 (Fig. S1). Subunit nomenclature for this family of enzymes differs between F-and V-type complexes and from organism to organism. Where the eukaryotic ATP synthase F 1 catalytic region consists of α 3 β 3 γδε, the V-ATPase V 1 catalytic region consists of B 3 A 3 DF with no equivalent of the ε-subunit. The catalytic A-subunit of V-ATPase is homologous to the F-type ATP synthas...

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mentioning

confidence: 99%

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

Lau

Rubinstein

2010

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

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“…This architecture is also observed in the high-resolution X-ray structure of the subunit c oligomer from Ilyobacter tartaricus (Meier et al 2005), even though the relative orientation of the two helices and the conformation of polar loop are somewhat different. A remarkable feature of the NMR solution structure is that the helices fold together even though the number of interhelical contacts that may stabilize the hairpin structure is relatively small.…”

Section: Resultsmentioning

confidence: 71%

“…Model structures of the subunit c oligomer in E. coli were calculated from the solution structure of the subunit c monomer and extensive intersubunit cross-linking data (Dmitriev et al 1999b;Rastogi and Girvin 1999). Recently, a high-resolution structure of the subunit c oligomer from Ilyobacter tartaricus was solved by X-ray crystallography (Meier et al 2005).…”

mentioning

confidence: 99%

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Dmitriev¹,

Fillingame²

2007

Protein Science

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We have tested the role of the polar loop of subunit c of the Escherichia coli ATP synthase in stabilizing the hairpin structure of this protein. The structure of the c 32-52 peptide corresponding to the cytoplasmic region of subunit c bound to the dodecylphosphocholine micelles was solved by high-resolution NMR. The region comprising residues 41-47 forms a well-ordered structure rather similar to the conformation of the polar loop region in the solution structure of the full-length subunit c and is flanked by short ahelical segments. This result suggests that the rigidity of the polar loop significantly contributes to the stability of the hairpin formed by the two helices of subunit c. This experimental system may be useful for NMR studies of interactions between subunit c and subunits g and e, which together form the rotor of the ATP synthase.

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“…The c-subunit has a hairpin structure, which is composed of two a-helices and a connecting loop. Crystal structures of the F 1 -c-ring (34,35) and isolated c-ring (36)(37)(38) revealed that the c-subunits form a ring complex by assembling in a circle with the C-terminus pointing outward and the connecting loop toward the F 1 side (cytoplasmic side in bacteria) (Fig. 4).…”

Section: Structure Of F Omentioning

confidence: 99%

Operation mechanism of F_oF₁‐adenosine triphosphate synthase revealed by its structure and dynamics

Iino¹,

Noji²

2013

IUBMB Life

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F o F 1 -Adenosine triphosphate (ATP) synthase, a complex of two rotary motor proteins, reversibly converts the electrochemical potential of protons across the cell membrane into phosphate transfer potential of ATP to provide the energy currency of the cell. The water-soluble motor is F 1 -ATPase, which possesses ATP synthesis/hydrolysis catalytic sites. Isolated F 1 hydrolyses ATP to rotate the rotary shaft against the stator ring. The membrane-embedded motor is F o , which is driven by proton flow down the proton electrochemical potential. In the F o F 1 complex, the direction of mechanical rotation, the chemical reaction, and the proton transport are determined by the relative amplitudes between the Gibbs free energy of the ATP hydrolysis reaction and the electrochemical potential of protons across the membrane. Therefore, F o F 1 -ATP synthase is a highly efficient molecular device in which the chemical, mechanical, and potential energies are tightly and reversibly converted. In this critical review, we summarize our latest knowledge about the operation mechanism of this sophisticated nanomachine, revealed by its structure and dynamics.

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Structure of the Rotor Ring of F-Type Na ⁺ -ATPase from Ilyobacter tartaricus

Cited by 360 publications

References 34 publications

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Operation mechanism of F_oF₁‐adenosine triphosphate synthase revealed by its structure and dynamics

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Structure of the Rotor Ring of F-Type Na + -ATPase from Ilyobacter tartaricus

Cited by 360 publications

References 34 publications

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V O motor

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V O motor

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Operation mechanism of FoF1‐adenosine triphosphate synthase revealed by its structure and dynamics

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Structure of the Rotor Ring of F-Type Na ⁺ -ATPase from Ilyobacter tartaricus

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound V _O motor

Operation mechanism of F_oF₁‐adenosine triphosphate synthase revealed by its structure and dynamics