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TitleStructural mechanisms of phospholipid activation of the human TPC2 channel.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateMar 12, 2019
AuthorsJi She / Weizhong Zeng / Jiangtao Guo / Qingfeng Chen / Xiao-Chen Bai / Youxing Jiang /
PubMed AbstractMammalian two-pore channels (TPCs) regulate the physiological functions of the endolysosome. Here we present cryo-EM structures of human TPC2 (HsTPC2), a phosphatidylinositol 3,5-bisphosphate (PI(3,5) ...Mammalian two-pore channels (TPCs) regulate the physiological functions of the endolysosome. Here we present cryo-EM structures of human TPC2 (HsTPC2), a phosphatidylinositol 3,5-bisphosphate (PI(3,5)P)-activated, Na selective channel, in the ligand-bound and apo states. The apo structure captures the closed conformation, while the ligand-bound form features the channel in both open and closed conformations. Combined with functional analysis, these structures provide insights into the mechanism of PI(3,5)P-regulated gating of TPC2, which is distinct from that of TPC1. Specifically, the endolysosome-specific PI(3,5)P binds at the first 6-TM and activates the channel - independently of the membrane potential - by inducing a structural change at the pore-lining inner helix (IS6), which forms a continuous helix in the open state but breaks into two segments at Gly317 in the closed state. Additionally, structural comparison to the voltage-dependent TPC1 structure allowed us to identify Ile551 as being responsible for the loss of voltage dependence in TPC2.
External linksElife / PubMed:30860481 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.7 Å
Structure data

0477

6nq0

EMDB-0477, PDB-6nq0:
Cryo-EM structure of human TPC2 channel in the ligand-bound open state
Method: EM (single particle) / Resolution: 3.7 Å

0478

6nq1

EMDB-0478, PDB-6nq1:
Cryo-EM structure of human TPC2 channel in the apo state
Method: EM (single particle) / Resolution: 3.5 Å

0479

6nq2

EMDB-0479, PDB-6nq2:
Cryo-EM structure of human TPC2 channel in the ligand-bound closed state
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-EUJ:
(2R)-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,4,6-trihydroxy-3,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dioctanoate

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / channel / lysosome

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