Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 113, Issue 12, Page 3245-3250, Year 2016
Publish date	Mar 22, 2016
Authors	Daniel G Schep / Jianhua Zhao / John L Rubinstein /
PubMed Abstract	Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the ...Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacterium Thermus thermophilus is similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined the T. thermophilus V/A-ATPase structure by cryo-EM at 6.4 Å resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequence within the map, providing a complete model of the rotary ATPase. Comparing the membrane-embedded regions of the T. thermophilus V/A-ATPase and eukaryotic V-ATPase from Saccharomyces cerevisiae allowed identification of the α-helices that belong to the a subunit and revealed the existence of previously unknown subunits in the eukaryotic enzyme. Subsequent evolutionary covariance analysis enabled construction of a model of the a subunit in the S. cerevisae V-ATPase that explains numerous biochemical studies of that enzyme. Comparing the two a subunit structures determined here with a structure of the distantly related a subunit from the bovine F-type ATP synthase revealed a conserved pattern of residues, suggesting a common mechanism for proton transport in all rotary ATPases.
External links	Proc Natl Acad Sci U S A / PubMed:26951669 / PubMed Central
Methods	EM (single particle)
Resolution	6.4 - 9.5 Å
Structure data	8016 5gar EMDB-8016, PDB-5gar: Thermus thermophilus V/A-ATPase, conformation 1 Method: EM (single particle) / Resolution: 6.4 Å 8017 5gas EMDB-8017, PDB-5gas: Thermus thermophilus V/A-ATPase, conformation 2 Method: EM (single particle) / Resolution: 9.5 Å 8070 5i1m EMDB-8070, PDB-5i1m: Yeast V-ATPase average of densities, a subunit segment Method: EM (single particle) / Resolution: 7.0 Å
Source	thermus thermophilus (bacteria) saccharomyces cerevisiae (brewer's yeast)
Keywords	HYDROLASE / V/A-ATPase / V-ATPase / A-ATPase / Thermus thermophilus / rotary ATPase / membrane protein / Vo region