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3V6I

Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase at 2.25 A resolution

Summary for 3V6I
Entry DOI10.2210/pdb3v6i/pdb
Related3K5B
DescriptorV-type ATP synthase subunit E, V-type ATP synthase, subunit (VAPC-THERM), CALCIUM ION, ... (5 entities in total)
Functional Keywordsperipheral stator stalk, right handed coiled-coil, atpase/synthase, atp binding, membrane, hydrolase
Biological sourceThermus thermophilus
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Total number of polymer chains4
Total formula weight64803.24
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 citationStewart, 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: 22353718
DOI: 10.1038/ncomms1693
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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