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TitleCryo-EM structure of the polyphosphate polymerase VTC reveals coupling of polymer synthesis to membrane transit.
Journal, issue, pagesEMBO J, Vol. 42, Issue 10, Page e113320, Year 2023
Publish dateMay 15, 2023
AuthorsWei Liu / Jiening Wang / Véronique Comte-Miserez / Mengyu Zhang / Xuejing Yu / Qingfeng Chen / Henning Jacob Jessen / Andreas Mayer / Shan Wu / Sheng Ye /
PubMed AbstractThe eukaryotic vacuolar transporter chaperone (VTC) complex acts as a polyphosphate (polyP) polymerase that synthesizes polyP from adenosine triphosphate (ATP) and translocates polyP across the ...The eukaryotic vacuolar transporter chaperone (VTC) complex acts as a polyphosphate (polyP) polymerase that synthesizes polyP from adenosine triphosphate (ATP) and translocates polyP across the vacuolar membrane to maintain an intracellular phosphate (P ) homeostasis. To discover how the VTC complex performs its function, we determined a cryo-electron microscopy structure of an endogenous VTC complex (Vtc4/Vtc3/Vtc1) purified from Saccharomyces cerevisiae at 3.1 Å resolution. The structure reveals a heteropentameric architecture of one Vtc4, one Vtc3, and three Vtc1 subunits. The transmembrane region forms a polyP-selective channel, likely adopting a resting state conformation, in which a latch-like, horizontal helix of Vtc4 limits the entrance. The catalytic Vtc4 central domain is located on top of the pseudo-symmetric polyP channel, creating a strongly electropositive pathway for nascent polyP that can couple synthesis to translocation. The SPX domain of the catalytic Vtc4 subunit positively regulates polyP synthesis by the VTC complex. The noncatalytic Vtc3 regulates VTC through a phosphorylatable loop. Our findings, along with the functional data, allow us to propose a mechanism of polyP channel gating and VTC complex activation.
External linksEMBO J / PubMed:37066886 / PubMed Central
MethodsEM (single particle)
Resolution3.06 Å
Structure data

35208

8i6v

EMDB-35208, PDB-8i6v:
Cryo-EM structure of the polyphosphate polymerase VTC complex(Vtc4/Vtc3/Vtc1)
Method: EM (single particle) / Resolution: 3.06 Å

Chemicals

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-3PO:
TRIPHOSPHATE

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMEMBRANE PROTEIN / polyphosphate polymerase; VTC complex; coupled synthesis and translocation

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