Structural and functional analysis of the coupling subunit F in solution and topological arrangement of the stalk domains of the methanogenic A1AO ATP synthase
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Summary
The first low-resolution shape of subunit F of the A1AO ATP synthase from the archaeon Methanosarcina mazei Gö1 in solution was determined by small angle X-ray scattering, demonstrating movements of subunits F relative to the nucleotide-binding subunit B.
- Type
- article
- Published
- 2006-08-03
- Cited by
- 36
- References
- 45
- OpenAlex
- https://openalex.org/W2012065740
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:46043924
Keywords
ATP synthase gamma subunit, ATP synthase, Protein subunit, Carbodiimide, Bioorganic chemistry
References
- The Protein Data Bank: a computer-based archival file for macromolecular structures.
- Structure and Subunit Arrangement of the A-type ATP Synthase Complex from the Archaeon Methanococcus jannaschii Visualized by Electron Microscopy*
- ATP Synthases in the Year 2000: Evolving Views about the Structures of These Remarkable Enzyme Complexes
- Isolation of a complete A1AO ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii
- Amino acid sequence of the alpha and beta subunits of Methanosarcina barkeri ATPase deduced from cloned genes. Similarity to subunits of eukaryotic vacuolar and F0F1-ATPases.
- Energy Conservation by the H2:Heterodisulfide Oxidoreductase from Methanosarcina mazei Gö1: Identification of Two Proton-Translocating Segments
- The structure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
- A comparison of an ATPase from the archaebacterium Halobacterium saccharovorum with the F1 moiety from the Escherichia coli ATP synthase.
- Defined subcomplexes of the A1 ATPase from the archaeon Methanosarcina mazei Gö1: biochemical properties and redox regulation
- Three-dimensional Map of a Plant V-ATPase Based on Electron Microscopy*
- PRIMUS: a Windows PC-based system for small-angle scattering data analysis
- Crystal Structure and Binding Properties of the Serratia marcescens Chitin-binding Protein CBP21*
- Structural analysis of the stalk subunit Vma5p of the yeast V‐ATPase in solution
- Post-translational Modifications of Endothelin Receptor B from Bovine Lungs Analyzed by Mass Spectrometry*
- Determination of domain structure of proteins from X-ray solution scattering.
- Data acquisition systems for linear and area X-ray detectors using delay line readout
- Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities.
- Structural Insights into the A1 ATPase from the archaeon, Methanosarcina mazei Gö1.
- Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B.
- Conformational Changes in the Escherichia coli ATP Synthase (ECF1F0) Monitored by Nucleotide-dependent Differences in the Reactivity of Cys-87 of the γ Subunit in the Mutant βGlu-381 → Ala*
Cited by
- Crystal and NMR Structures Give Insights into the Role and Dynamics of Subunit F of the Eukaryotic V-ATPase from Saccharomyces cerevisiae*
- MALDI-ToF mass spectrometry for studying noncovalent complexes of biomolecules.
- Identification of critical residues of subunit H in its interaction with subunit E of the A‐ATP synthase from Methanocaldococcus jannaschii
- Life close to the thermodynamic limit: how methanogenic archaea conserve energy.
- ATP/ADP Binding to a Novel Nucleotide Binding Domain of the Reticulocyte-binding Protein Py235 of Plasmodium yoelii*
- NMR solution structure of the N-terminal domain of subunit E (E1–52) of A1AO ATP synthase from Methanocaldococcus jannaschii
- A second transient position of ATP on its trail to the nucleotide-binding site of subunit B of the motor protein A(1)A(0) ATP synthase.
- The stator complex of the A1A0-ATP synthase--structural characterization of the E and H subunits.
- Solution structure of subunit F (Vma7p) of the eukaryotic V(1)V(O) ATPase from Saccharomyces cerevisiae derived from SAXS and NMR spectroscopy.
- Nucleotide binding states of subunit A of the A-ATP synthase and the implication of P-loop switch in evolution.
- Disulfide linkage in the coiled‐coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C‐terminal segment H85–104
- Binding of subunit E into the A-B interface of the A(1)A(O) ATP synthase.
- Interaction of the Thermoplasma acidophilum A1A0-ATP synthase peripheral stalk with the catalytic domain
- Three-dimensional Structure of A1A0 ATP Synthase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Electron Microscopy*
- Structure of the nucleotide-binding subunit B of the energy producer A1A0 ATP synthase in complex with adenosine diphosphate.
- The structure of subunit E of the Pyrococcus horikoshii OT3 A-ATP synthase gives insight into the elasticity of the peripheral stalk.
- Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47).
- Crystal and solution structure of the C-terminal part of the Methanocaldococcus jannaschii A1AO ATP synthase subunit E revealed by X-ray diffraction and small-angle X-ray scattering
- Spectroscopic and crystallographic studies of the mutant R416W give insight into the nucleotide binding traits of subunit B of the A1Ao ATP synthase
- ATP synthases from archaea: the beauty of a molecular motor.
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