3V6I
Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase at 2.25 A resolution
Summary for 3V6I
| Entry DOI | 10.2210/pdb3v6i/pdb |
| Related | 3K5B |
| Descriptor | V-type ATP synthase subunit E, V-type ATP synthase, subunit (VAPC-THERM), CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | peripheral stator stalk, right handed coiled-coil, atpase/synthase, atp binding, membrane, hydrolase |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 4 |
| Total formula weight | 64803.24 |
| Authors | Stewart, A.G.,Lee, L.K.,Donohoe, M.,Chaston, J.J.,Stock, D. (deposition date: 2011-12-19, release date: 2012-02-22, Last modification date: 2024-03-20) |
| Primary citation | Stewart, A.G.,Lee, L.K.,Donohoe, M.,Chaston, J.J.,Stock, D. The dynamic stator stalk of rotary ATPases Nat Commun, 3:687-687, 2012 Cited by PubMed Abstract: Rotary ATPases couple ATP hydrolysis/synthesis with proton translocation across biological membranes and so are central components of the biological energy conversion machinery. Their peripheral stalks are essential components that counteract torque generated by rotation of the central stalk during ATP synthesis or hydrolysis. Here we present a 2.25-Å resolution crystal structure of the peripheral stalk from Thermus thermophilus A-type ATPase/synthase. We identify bending and twisting motions inherent within the structure that accommodate and complement a radial wobbling of the ATPase headgroup as it progresses through its catalytic cycles, while still retaining azimuthal stiffness necessary to counteract rotation of the central stalk. The conformational freedom of the peripheral stalk is dictated by its unusual right-handed coiled-coil architecture, which is in principle conserved across all rotary ATPases. In context of the intact enzyme, the dynamics of the peripheral stalks provides a potential mechanism for cooperativity between distant parts of rotary ATPases. PubMed: 22353718DOI: 10.1038/ncomms1693 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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