5Y60

V/A-type ATPase/synthase from Thermus thermophilus, rotational state 3.

Summary for 5Y60

• Entry DOI: 10.2210/pdb5y60/pdb
• EMDB information: 6813
• Descriptor: V-type ATP synthase alpha chain, ADENOSINE-5'-DIPHOSPHATE, V-type ATP synthase beta chain, ... (10 entities in total)
• Functional Keywords: atp synthase, proton pump, v-atpase, bioenergetics, motor protein
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 26
• Total formula weight: 681628.56

Authors

Nakanishi, A.,Kishikawa, J.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. (deposition date: 2017-08-10, release date: 2018-01-17, Last modification date: 2024-03-27)

Primary citation

Nakanishi, A.,Kishikawa, J.I.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K.
Cryo EM structure of intact rotary H+-ATPase/synthase from Thermus thermophilus
Nat Commun, 9:89-89, 2018

PubMed Abstract: Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H-rotary ATPase from the bacterium Thermus thermophilus, enabling the identification of three rotational states based on the orientation of the rotor subunit. Using masked refinement and classification with signal subtractions, we obtain homogeneous reconstructions for the whole complexes and soluble V domains. These reconstructions are of higher resolution than any EM map of intact rotary ATPase reported previously, providing a detailed molecular basis for how the rotary ATPase maintains structural integrity of the peripheral stator apparatus, and confirming the existence of a clear proton translocation path from both sides of the membrane.

PubMed: 29311594
DOI: 10.1038/s41467-017-02553-6

Experimental method

ELECTRON MICROSCOPY (7.5 Å)