6R0Z

Thermus thermophilus V/A-type ATPase/synthase, rotational state 1L

Summary for 6R0Z

• Entry DOI: 10.2210/pdb6r0z/pdb
• Related: 6QUM 6R0W 6R0Y 6R10
• EMDB information: 4640 4699 4700 4702 4703
• Descriptor: V-type ATP synthase alpha chain, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (11 entities in total)
• Functional Keywords: atp hydrolysis/synthesis, proton translocation, rotary catalysis, membrane protein
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 26
• Total formula weight: 681544.64

Authors

Zhou, L.,Sazanov, L. (deposition date: 2019-03-13, release date: 2019-08-28, Last modification date: 2024-05-15)

Primary citation

Zhou, L.,Sazanov, L.A.
Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
Science, 365:-, 2019

PubMed Abstract: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V and V in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V-V torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family.

PubMed: 31439765
DOI: 10.1126/science.aaw9144

Experimental method

ELECTRON MICROSCOPY (3.8 Å)