4DL0

Crystal Structure of the heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase

Summary for 4DL0

• Entry DOI: 10.2210/pdb4dl0/pdb
• Descriptor: V-type proton ATPase subunit C, V-type proton ATPase subunit G, V-type proton ATPase subunit E, ... (6 entities in total)
• Functional Keywords: coiled-coil, heterotrimer, peripheral stalk, stator complex, hydrolase, ion transport, vacuolar atpase, vacuolar membrane
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Vacuole membrane ; Peripheral membrane protein : P31412 P22203
• Total number of polymer chains: 6
• Total formula weight: 109899.44

Authors

Oot, R.A.,Huang, L.S.,Berry, E.A.,Wilkens, S. (deposition date: 2012-02-05, release date: 2012-10-10, Last modification date: 2024-02-28)

Primary citation

Oot, R.A.,Huang, L.S.,Berry, E.A.,Wilkens, S.
Crystal Structure of the Yeast Vacuolar ATPase Heterotrimeric EGC(head) Peripheral Stalk Complex.
Structure, 20:1881-1892, 2012

PubMed 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.

PubMed: 23000382
DOI: 10.1016/j.str.2012.08.020

Experimental method

X-RAY DIFFRACTION (2.905 Å)