Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance
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Summary
The structure of the V/A-ATPase from the eubacterium Thermus thermophilus is determined, suggesting a common mechanism for proton transport in all rotary ATPases.
- Type
- article
- Published
- 2016-03-07
- Cited by
- 49
- References
- 65
- Access
- Open access
- OpenAlex
- https://openalex.org/W2294124032
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1034170
Keywords
Thermus thermophilus, ATPase, Protein subunit, V-ATPase, Biology
References
- Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
- Protein Structure Prediction Using Rosetta
- Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing
- STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p.
- Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness
- A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit.
- Interaction between Glu-219 and His-245 within the a subunit of F1F0-ATPase in Escherichia coli.
- Defects in TCIRG1 subunit of the vacuolar proton pump are responsible for a subset of human autosomal recessive osteopetrosis
- Description and comparison of algorithms for correcting anisotropic magnification in cryo-EM images.
- Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo.
- Alignment of cryo-EM movies of individual particles by optimization of image translations.
- The Phyre2 web portal for protein modelling, prediction and analysis
- Function of a Subunit Isoforms of the V-ATPase in pH Homeostasis and in Vitro Invasion of MDA-MB231 Human Breast Cancer Cells*
- Analysis of the Membrane Topology of Transmembrane Segments in the C-terminal Hydrophobic Domain of the Yeast Vacuolar ATPase Subunit a (Vph1p) by Chemical Modification*
- Crystal structure of the cytoplasmic N-terminal domain of subunit I, a homolog of subunit a, of V-ATPase
- Refinement of Protein Structures into Low-Resolution Density Maps using Rosetta
- Transmembrane Topography of the 100-kDa a Subunit (Vph1p) of the Yeast Vacuolar Proton-translocating ATPase*
- Osteoclastic bone resorption by a polarized vacuolar proton pump.
- ATP synthase: an electrochemical transducer with rotatory mechanics.
- Site-directed Mutagenesis of the 100-kDa Subunit (Vph1p) of the Yeast Vacuolar (H+)-ATPase*
Cited by
- Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases
- The changing landscape of membrane protein structural biology through developments in electron microscopy
- Atomic model for the membrane-embedded VO motor of a eukaryotic V-ATPase
- Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states
- Cryo-EM analysis of a domain antibody bound rotary ATPase complex.
- Protein Structure Determination using Metagenome sequence data
- EM as a tool to study structure and function to guide inhibitor design
- Applications of contact predictions to structural biology
- Recent developments in the CCP-EM software suite
- N‐linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+‐ATPase (V‐ATPase) biosynthesis
- Dissociation and purification of the endogenous membrane-bound Vo complex from Pichia pastoris.
- Applications of sequence coevolution in membrane protein biochemistry
- Atomic model for the dimeric FO region of mitochondrial ATP synthase
- Molecular mechanisms of cutis laxa– and distal renal tubular acidosis–causing mutations in V-ATPase a subunits, ATP6V0A2 and ATP6V0A4
- Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase.
- Cryo-EM of ATP synthases.
- The Peripheral Stalk of Rotary ATPases
- Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy
- Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
- Insights into water accessible pathways and the inactivation mechanism of proton translocation by the membrane-embedded domain of V-type ATPases.
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- AtpΘ is an inhibitor of F0F1 ATP synthase to arrest ATP hydrolysis during low-energy conditions in cyanobacteria
- The F Subunit of Thermus thermophilus V1-ATPase Promotes ATPase Activity but Is Not Necessary for Rotation*
- The Spatio-Temporal Organization of Mitochondrial F1FO-ATP Synthase Is Determined by its Activity and Controlled by IF1
- [Evolutonary modifications of molecular structure of ATP-synthase gamma-subunit].
- ATP synthases from archaea: the beauty of a molecular motor.