6M0S

3.6A Yeast Vo state3 prime

Summary for 6M0S

• Entry DOI: 10.2210/pdb6m0s/pdb
• EMDB information: 30035
• Descriptor: V-type proton ATPase subunit a, vacuolar isoform, V-type proton ATPase subunit e, Uncharacterized protein YPR170W-B, ... (8 entities in total)
• Functional Keywords: v-atpase, vo sub-complex, rotary motor, transport protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 15
• Total formula weight: 322869.04

Authors

Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,SIngharoy, A.,Chiu, W. (deposition date: 2020-02-22, release date: 2020-11-04, Last modification date: 2024-03-27)

Primary citation

Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,Singharoy, A.,Chiu, W.
Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of V o complex.
Sci Adv, 6:-, 2020

PubMed Abstract: Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a V proton channel subcomplex. Despite recent high-resolution structures of several rotary ATPases, the dynamic mechanism of proton pumping remains elusive. Here, we determined a 2.7-Å cryo-electron microscopy (cryo-EM) structure of yeast V proton channel in nanodisc that reveals the location of ordered water molecules along the proton path, details of specific protein-lipid interactions, and the architecture of the membrane scaffold protein. Moreover, we uncover a state of V that shows the -ring rotated by ~14°. Molecular dynamics simulations demonstrate that the two rotary states are in thermal equilibrium and depict how the protonation state of essential glutamic acid residues couples water-mediated proton transfer with -ring rotation. Our cryo-EM models and simulations also rationalize a mechanism for inhibition of passive proton transport as observed for free V that is generated as a result of V-ATPase regulation by reversible disassembly in vivo.

PubMed: 33028525
DOI: 10.1126/sciadv.abb9605

Experimental method

ELECTRON MICROSCOPY (3.6 Å)