5I1M
Yeast V-ATPase average of densities, a subunit segment
Summary for 5I1M
| Entry DOI | 10.2210/pdb5i1m/pdb |
| Related | 5GAR 5GAS |
| EMDB information | 8016 8017 8070 |
| Descriptor | V-type proton ATPase subunit a, vacuolar isoform (1 entity in total) |
| Functional Keywords | v-atpase, vo region, membrane protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 51548.87 |
| Authors | Schep, D.G.,Zhao, J.,Rubinstein, J.L. (deposition date: 2016-02-05, release date: 2016-03-09, Last modification date: 2024-03-06) |
| Primary citation | Schep, D.G.,Zhao, J.,Rubinstein, J.L. Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance. Proc.Natl.Acad.Sci.USA, 113:3245-3250, 2016 Cited by 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 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. PubMed: 26951669DOI: 10.1073/pnas.1521990113 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
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