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TitleCoupling sensor to enzyme in the voltage sensing phosphatase.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 6409, Year 2024
Publish dateJul 30, 2024
AuthorsYawei Yu / Lin Zhang / Baobin Li / Zhu Fu / Stephen G Brohawn / Ehud Y Isacoff /
PubMed AbstractVoltage-sensing phosphatases (VSPs) dephosphorylate phosphoinositide (PIP) signaling lipids in response to membrane depolarization. VSPs possess an S4-containing voltage sensor domain (VSD), ...Voltage-sensing phosphatases (VSPs) dephosphorylate phosphoinositide (PIP) signaling lipids in response to membrane depolarization. VSPs possess an S4-containing voltage sensor domain (VSD), resembling that of voltage-gated cation channels, and a lipid phosphatase domain (PD). The mechanism by which voltage turns on enzyme activity is unclear. Structural analysis and modeling suggest several sites of VSD-PD interaction that could couple voltage sensing to catalysis. Voltage clamp fluorometry reveals voltage-driven rearrangements in three sites implicated earlier in enzyme activation-the VSD-PD linker, gating loop and R loop-as well as the N-terminal domain, which has not yet been explored. N-terminus mutations perturb both rearrangements in the other segments and enzyme activity. Our results provide a model for a dynamic assembly by which S4 controls the catalytic site.
External linksNat Commun / PubMed:39080263 / PubMed Central
MethodsEM (single particle)
Resolution2.97 Å
Structure data

45178

9c49

EMDB-45178, PDB-9c49:
Cryo-EM structure of Danio rerio voltage-sensing phosphatase (VSP) phosphatase domain
Method: EM (single particle) / Resolution: 2.97 Å

Source
  • danio rerio (zebrafish)
KeywordsMEMBRANE PROTEIN / phosphatase / voltage-sensing

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