Structure of the Membrane Domain of Subunit b of theEscherichia coli F0F1 ATP Synthase

Dmitriev, Oleg Y.; Jones, Phillip W.; Jiang, Weiping; Fillingame, Robert H.

doi:10.1074/jbc.274.22.15598

Cited by 136 publications

(140 citation statements)

References 56 publications

(45 reference statements)

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“…It is below the threshold level for membrane spanning segments, however, because this hydrophobic region (residues 29-45) is aligned with the predicted transmembrane segment of subunit b 1 (residues 11-29) it is likely that both b subunits possess a membrane spanning N-terminal segment, which anchors them in the membrane. This suggestion is in agreement with that of Dmitriev et al [10] who proposed a model for a b-b homodimer in the second stalk of the E. coli F 1 F 0 ATP synthase based upon two-dimensional 1 H NMR. The structure of the N-terminal transmembrane domain (residues 4-22) was suggested to form an a-helix that spans the membrane.…”

Section: Purification Of F 1 F 0 Atp Synthasesupporting

confidence: 92%

“…Functionally and structurally it can be divided into two parts, which can be isolated as separate entities: the membrane intrinsic F 0 and the peripheral F 1 . The subunit composition of this enzyme is a 3 b 3 cdeab 2 c [10][11][12][13][14] with a 3 b 3 cde constituting F 1 , and ab 2 c 10-14 forming F 0 [4]. The F 1 and F 0 parts are connected by a central stalk, composed of the c and e subunits, and a peripheral stalk, made of the d and b subunits [5,6].…”

Section: Introductionmentioning

confidence: 99%

“…Since the high resolution structure of the mitochondrial F 1 ATPase was reported [8] one of the main areas of interest has been the second stalk linking the F 1 and F 0 domains [9]. It is believed to function as a stator preventing the a 3 b 3 subunits from rotating together with c and e. Studies on the F 1 F 0 ATP synthase from E. coli have revealed the presence of two copies of subunit b forming the second stalk [10,11]. The roles and properties of subunit b within the F 1 F 0 ATP synthase have been investigated [12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

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Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

et al. 2006

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The F 1 F 0 ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits a, b, c, d and e of F 1 and subunits a and c of F 0 . Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F 1 and F 0 . In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the d subunit.

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Section: Purification Of F 1 F 0 Atp Synthasesupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

et al. 2006

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“…Thus, this portion of the stator stalk might have some flexibility, allowing bending motions which could serve as elastic element in the coupling machinery. In the case of the E. coli enzyme, a bend was detected at the C-terminus of the transmembrane helix [8], which could facilitate variations of the angle between the transmembrane helix and the long, cytoplasmic helix [14].…”

Section: The Function Of the Stator Stalkmentioning

confidence: 99%

“…1). Despite the progress in the structural analysis of other parts of ATP synthase, a high-resolution structural model of the stator stalk has been lacking so far, with available data limited to a few fragments of the stalk [5][6][7][8][9]. Now the situation has markedly improved with the publication of the x-ray structure of a major portion of the stator stalk of mitochondrial ATP synthase by Kane Dickson et al [10].…”

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ATP synthase – the structure of the stator stalk

Weber

2007

Trends in Biochemical Sciences

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ATP synthase synthesizes ATP from ADP and inorganic phosphate by a unique rotary mechanism where two subcomplexes move relative to each other, powered by a proton or sodium gradient. The non-rotating parts of the machinery are held together by the "stator stalk". Significant progress towards a structural model for the holoenzyme was made recently, when the structure of a major portion of the stator stalk of mitochondrial ATP synthase was resolved. ATP synthase -an overviewThe final step in oxidative phosphorylation and photophosphorylation, the synthesis of ATP from ADP and inorganic phosphate, is catalyzed by F 1 F o -ATP synthase. The driving force for ATP synthesis is a transmembrane proton (or, in some organisms, sodium ion) gradient. Coupling between proton flow and ATP synthesis is achieved by a unique rotary mechanism (for recent reviews, see [1][2][3]; for a historical perspective, see [4]). ATP synthase consists of two connected rotary motors. Flow of protons, down the gradient, through the F o motor drives rotation of the ring of c subunits of the rotor (Fig. 1). The c ring connects to subunit γ. Rotation of γ causes conformational changes in the catalytic nucleotide binding sites on the three β subunits of the F 1 motor, resulting in synthesis and release of ATP. However, this can only happen if the non-rotating, static portions of both motors are affixed to each other, to prevent co-rotation of the α 3 β 3 ring with the γ subunit. This attachment is achieved via the "stator stalk" (Fig. 1). Despite the progress in the structural analysis of other parts of ATP synthase, a high-resolution structural model of the stator stalk has been lacking so far, with available data limited to a few fragments of the stalk [5][6][7][8][9]. Now the situation has markedly improved with the publication of the x-ray structure of a major portion of the stator stalk of mitochondrial ATP synthase by Kane Dickson et al. [10]. The structure of the stator stalk of mitochondrial ATP synthaseIn the mitochondrial enzyme the stator stalk consists of one copy each of subunits b, d, F 6 and OSCP (the "oligomycin-sensitivity conferring protein", homologous to bacterial subunit δ in NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript of the b helix, and are followed by an extended region that stretches near to the middle of b (Fig. 2).Kane Dickson et al. [10] demonstrate that, together with the structures of the F 1 c 10 complex [11] and of the N-terminal domain of OSCP [6], the structure of the b/d/F 6 subcomplex fits very well into a 32 Å resolution structure of mitochondrial ATP synthase obtained by cryoelectron microscopy [12]. The N-terminus of the portion of the b subunit included in the crystallized b/d/F 6 subcomplex is located very close to the transmembrane region of the enzyme. The curvature of the stator stalk follows the outer surface of the α 3 β 3 ring, and the end with the C-terminus of the long b helix and the N-terminus of F 6 comes close to the "top" of F 1 , where O...

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Proton Translocating ATPases

Futai

Sun‐Wada

Wada

2006

Encyclopedia of Molecular Cell Biology and Molecular Medicine

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Structure of the Membrane Domain of Subunit b of theEscherichia coli F0F1 ATP Synthase

Cited by 136 publications

References 56 publications

Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

ATP synthase – the structure of the stator stalk

Proton Translocating ATPases

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Structure of the Membrane Domain of Subunit b of theEscherichia coli F0F1 ATP Synthase

Cited by 136 publications

References 56 publications

Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

Biochemical and electron microscopic characterization of the F1F0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

ATP synthase – the structure of the stator stalk

Proton Translocating ATPases

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Product

Resources

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Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus

Biochemical and electron microscopic characterization of the F₁F₀ ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus