3J9U

Yeast V-ATPase state 2

Summary for 3J9U

• Entry DOI: 10.2210/pdb3j9u/pdb
• Related: 3J9T 3J9V
• EMDB information: 6284 6285 6286
• Descriptor: V-type proton ATPase subunit D, V-type proton ATPase subunit C, V-type proton ATPase subunit c, ... (11 entities in total)
• Functional Keywords: v-atpase, v-type atpase, vacuolar-type atpase, proton pump, hydrolase
• Biological source: Saccharomyces cerevisiae (yeast); More
• Total number of polymer chains: 28
• Total formula weight: 934643.41

Authors

Zhao, J.,Benlekbir, S.,Rubinstein, J.L. (deposition date: 2015-02-23, release date: 2015-05-13, Last modification date: 2024-02-21)

Primary citation

Zhao, J.,Benlekbir, S.,Rubinstein, J.L.
Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase.
Nature, 521:241-245, 2015

PubMed Abstract: Eukaryotic vacuolar H(+)-ATPases (V-ATPases) are rotary enzymes that use energy from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of many intracellular compartments. ATP hydrolysis in the soluble catalytic region of the enzyme is coupled to proton translocation through the membrane-bound region by rotation of a central rotor subcomplex, with peripheral stalks preventing the entire membrane-bound region from turning with the rotor. The eukaryotic V-ATPase is the most complex rotary ATPase: it has three peripheral stalks, a hetero-oligomeric proton-conducting proteolipid ring, several subunits not found in other rotary ATPases, and is regulated by reversible dissociation of its catalytic and proton-conducting regions. Studies of ATP synthases, V-ATPases, and bacterial/archaeal V/A-ATPases have suggested that flexibility is necessary for the catalytic mechanism of rotary ATPases, but the structures of different rotational states have never been observed experimentally. Here we use electron cryomicroscopy to obtain structures for three rotational states of the V-ATPase from the yeast Saccharomyces cerevisiae. The resulting series of structures shows ten proteolipid subunits in the c-ring, setting the ATP:H(+) ratio for proton pumping by the V-ATPase at 3:10, and reveals long and highly tilted transmembrane α-helices in the a-subunit that interact with the c-ring. The three different maps reveal the conformational changes that occur to couple rotation in the symmetry-mismatched soluble catalytic region to the membrane-bound proton-translocating region. Almost all of the subunits of the enzyme undergo conformational changes during the transitions between these three rotational states. The structures of these states provide direct evidence that deformation during rotation enables the smooth transmission of power through rotary ATPases.

PubMed: 25971514
DOI: 10.1038/nature14365

Experimental method

ELECTRON MICROSCOPY (7.6 Å)