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Structure paper

TitleCoordinated conformational changes in the V complex during V-ATPase reversible dissociation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 5, Page 430-439, Year 2022
Publish dateApr 25, 2022
AuthorsThamiya Vasanthakumar / Kristine A Keon / Stephanie A Bueler / Michael C Jaskolka / John L Rubinstein /
PubMed AbstractVacuolar-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 ...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.
External linksNat Struct Mol Biol / PubMed:35469063
MethodsEM (single particle)
Resolution3.3 - 3.8 Å
Structure data

25996

7tmm

EMDB-25996, PDB-7tmm:
Complete V1 Complex from Saccharomyces cerevisiae
Method: EM (single particle) / Resolution: 3.5 Å

25997

7tmo

EMDB-25997, PDB-7tmo:
V1 complex lacking subunit C from Saccharomyces cerevisiae, State 1
Method: EM (single particle) / Resolution: 3.3 Å

25998

7tmp

EMDB-25998, PDB-7tmp:
V1 complex lacking subunit C from Saccharomyces cerevisiae, State 2
Method: EM (single particle) / Resolution: 3.3 Å

25999

7tmq

EMDB-25999, PDB-7tmq:
V1 complex lacking subunit C from Saccharomyces cerevisiae, State 3
Method: EM (single particle) / Resolution: 3.3 Å

26000

7tmr

EMDB-26000, PDB-7tmr:
V-ATPase from Saccharomyces cerevisiae, State 1
Method: EM (single particle) / Resolution: 3.5 Å

26001

7tms

EMDB-26001, PDB-7tms:
V-ATPase from Saccharomyces cerevisiae, State 2
Method: EM (single particle) / Resolution: 3.8 Å

26002

7tmt

EMDB-26002, PDB-7tmt:
V-ATPase from Saccharomyces cerevisiae, State 3
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsHYDROLASE / V-ATPase / MEMBRANE PROTEIN

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