Soung-Hun Roh / Nicholas J Stam / Corey F Hryc / Sergio Couoh-Cardel / Grigore Pintilie / Wah Chiu / Stephan Wilkens /
PubMed Abstract
The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-Å resolution cryoEM structure of the lipid nanodisc- ...The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-Å resolution cryoEM structure of the lipid nanodisc-reconstituted V proton channel of the yeast vacuolar H-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton pathway at the interface of the proteolipid ring and subunit a. Based on the structure and previous mutagenesis studies, we propose the chemical basis of transmembrane proton transport. Moreover, we discovered that the C terminus of the assembly factor Voa1 is an integral component of mature V. Voa1's C-terminal transmembrane α helix is bound inside the proteolipid ring, where it contributes to the stability of the complex. Our structure rationalizes possible mechanisms by which mutations in human V can result in disease phenotypes and may thus provide new avenues for therapeutic interventions.
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Keywords
MEMBRANE PROTEIN / Vacuolar H+-ATPase / Vo proton channel / rotary motor enzyme
