3K5B
Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase
Summary for 3K5B
| Entry DOI | 10.2210/pdb3k5b/pdb |
| Descriptor | V-type ATP synthase, subunit (VAPC-THERM), V-type ATP synthase subunit E (2 entities in total) |
| Functional Keywords | right handed coiled coil, vacuolar atpase/synthase, v-type atpase/synthase, a-type atpase/synthase, peripheral stator, peripheral stalk, atp synthesis, hydrogen ion transport, ion transport, transport, hydrolase |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 4 |
| Total formula weight | 65111.04 |
| Authors | Lee, L.K.,Stewart, A.G.,Donohoe, M.,Bernal, R.A.,Stock, D. (deposition date: 2009-10-07, release date: 2010-02-23, Last modification date: 2024-10-09) |
| Primary citation | Lee, L.K.,Stewart, A.G.,Donohoe, M.,Bernal, R.A.,Stock, D. The structure of the peripheral stalk of Thermus thermophilus H(+)-ATPase/synthase. Nat.Struct.Mol.Biol., 17:373-378, 2010 Cited by PubMed Abstract: Proton-translocating ATPases are ubiquitous protein complexes that couple ATP catalysis with proton translocation via a rotary catalytic mechanism. The peripheral stalks are essential components that counteract torque generated from proton translocation during ATP synthesis or from ATP hydrolysis during proton pumping. Despite their essential role, the peripheral stalks are the least conserved component of the complexes, differing substantially between subtypes in composition and stoichiometry. We have determined the crystal structure of the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus consisting of subunits E and G. The structure contains a heterodimeric right-handed coiled coil, a protein fold never observed before. We have fitted this structure into the 23 A resolution EM density of the intact A-ATPase complex, revealing the precise location of the peripheral stalk and new implications for the function and assembly of proton-translocating ATPases. PubMed: 20173764DOI: 10.1038/nsmb.1761 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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