7TMQ

V1 complex lacking subunit C from Saccharomyces cerevisiae, State 3

Summary for 7TMQ

• Entry DOI: 10.2210/pdb7tmq/pdb
• Related: 7TMM 7TMO 7TMP 7TMR 7TMS 7TMT
• EMDB information: 25996 25997 25998 25999 26000 26001 26002
• Descriptor: H(+)-transporting two-sector ATPase, Vacuolar proton pump subunit B, V-type proton ATPase subunit E, ... (9 entities in total)
• Functional Keywords: hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 15
• Total formula weight: 600380.28

Authors

Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L. (deposition date: 2022-01-19, release date: 2022-04-06, Last modification date: 2024-02-21)

Primary citation

Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L.
Coordinated conformational changes in the V 1 complex during V-ATPase reversible dissociation.
Nat.Struct.Mol.Biol., 29:430-439, 2022

PubMed Abstract: Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V region that hydrolyzes ATP and a membrane-embedded V region that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V and V complexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V. In yeast, assembly of the V and V regions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V complex and the V complex lacking subunit C. On separation, V undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with V. Loss of subunit C allows V to match the rotational state of V, suggesting how RAVE could reassemble V and V by recruiting subunit C.

PubMed: 35469063
DOI: 10.1038/s41594-022-00757-z

Experimental method

ELECTRON MICROSCOPY (3.3 Å)