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PMID: 23000382 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.

Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex.

Structure (London, England : 1993) ·Vol. 20 ·No. 11 ·2012-11-07 ·Pages 1881-92

Oot RA, Huang LS, Berry EA, Wilkens S

Abstract

Vacuolar ATPases (V-ATPases) are multisubunit rotary motor proton pumps that function to acidify subcellular organelles in all eukaryotic organisms. V-ATPase is regulated by a unique mechanism that involves reversible dissociation into V₁-ATPase and V₀ proton channel, a process that involves breaking of protein interactions mediated by subunit C, the cytoplasmic domain of subunit "a" and three "peripheral stalks," each made of a heterodimer of E and G subunits. Here, we present crystal structures of a yeast V-ATPase heterotrimeric complex composed of EG heterodimer and the head domain of subunit C (C(head)). The structures show EG heterodimer folded in a noncanonical coiled coil that is stabilized at its N-terminal ends by binding to C(head). The coiled coil is disrupted by a bulge of partially unfolded secondary structure in subunit G and we speculate that this unique feature in the eukaryotic V-ATPase peripheral stalk may play an important role in enzyme structure and regulation by reversible dissociation.

MeSH Terms
Amino Acid Sequence Crystallography, X-Ray Dimerization Models, Molecular Molecular Sequence Data Protein Conformation Saccharomyces cerevisiae/enzymology Vacuolar Proton-Translocating ATPases/chemistry,metabolism
Chemicals
Vacuolar Proton-Translocating ATPases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Oot Rebecca A
Department of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, Syracuse, NY 13210, USA.
Huang Li-Shar
Berry Edward A
Wilkens Stephan
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Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
1878-4186
DOI
10.1016/j.str.2012.08.020
Published
2012-11-07
Epub
2012-00-20
Pages
1881-92
Language
English
Region
United States
NLM ID
101087697
PMCID
PMC3496068
Subset
IM
Grants
NIGMS NIH HHS · GM103485 · United States
NIGMS NIH HHS · P41 GM103485 · United States
NIGMS NIH HHS · R01 GM058600 · United States
NIGMS NIH HHS · GM058600 · United States
NCRR NIH HHS · P41 RR001646 · United States
Corrections
CommentIn
PMID: 23141690
External Links
PubMed source DOI: 10.1016/j.str.2012.08.020 PMC Full Text View journal details
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