6LY8

V/A-ATPase from Thermus thermophilus, the soluble domain, including V1, d, two EG stalks, and N-terminal domain of a-subunit.

Summary for 6LY8

• Entry DOI: 10.2210/pdb6ly8/pdb
• EMDB information: 30014
• Descriptor: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (5 entities in total)
• Functional Keywords: rotary atpase, v/a-atpase, molecular motor, motor protein
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 8
• Total formula weight: 387196.11

Authors

Kishikawa, J.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. (deposition date: 2020-02-13, release date: 2020-09-09, Last modification date: 2020-09-30)

Primary citation

Kishikawa, J.I.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K.
Mechanical inhibition of isolated V o from V/A-ATPase for proton conductance.
Elife, 9:-, 2020

PubMed Abstract: V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V domain, the V domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the V domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the V/A-ATPase and isolated V at near-atomic resolution, respectively. These structures clarify how the isolated V domain adopts the auto-inhibited form and how the complex prevents formation of the inhibited V form.

PubMed: 32639230
DOI: 10.7554/eLife.56862

Experimental method

ELECTRON MICROSCOPY (3.5 Å)