4EFA

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

Summary for 4EFA

• Entry DOI: 10.2210/pdb4efa/pdb
• Related: 4DL0
• Descriptor: V-type proton ATPase subunit C, V-type proton ATPase subunit G, V-type proton ATPase subunit E, ... (5 entities in total)
• Functional Keywords: heterotrimer, peripheral stalk, vacuolar atpase, hydrolase
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Vacuole membrane ; Peripheral membrane protein : P31412 P22203
• Total number of polymer chains: 3
• Total formula weight: 54697.42

Authors

Oot, R.A.,Huang, L.S.,Berry, E.A.,Wilkens, S. (deposition date: 2012-03-29, release date: 2012-10-10, Last modification date: 2023-09-13)

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 (2.8163 Å)