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Structure paper

TitleGating of human TRPV3 in a lipid bilayer.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 7, Page 635-644, Year 2020
Publish dateJun 22, 2020
AuthorsZengqin Deng / Grigory Maksaev / Michael Rau / Zili Xie / Hongzhen Hu / James A J Fitzpatrick / Peng Yuan /
PubMed AbstractThe transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin ...The transient receptor potential cation channel subfamily V member 3 (TRPV3) channel plays a critical role in skin physiology, and mutations in TRPV3 result in the development of a congenital skin disorder, Olmsted syndrome. Here we describe multiple cryo-electron microscopy structures of human TRPV3 reconstituted into lipid nanodiscs, representing distinct functional states during the gating cycle. The ligand-free, closed conformation reveals well-ordered lipids interacting with the channel and two physical constrictions along the ion-conduction pore involving both the extracellular selectivity filter and intracellular helix bundle crossing. Both the selectivity filter and bundle crossing expand upon activation, accompanied by substantial structural rearrangements at the cytoplasmic intersubunit interface. Transition to the inactivated state involves a secondary structure change of the pore-lining helix, which contains a π-helical segment in the closed and open conformations, but becomes entirely α-helical upon inactivation. Together with electrophysiological characterization, structures of TRPV3 in a lipid membrane environment provide unique insights into channel activation and inactivation mechanisms.
External linksNat Struct Mol Biol / PubMed:32572252 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.33 Å
Structure data

20917

6uw4

EMDB-20917, PDB-6uw4:
Cryo-EM structure of human TRPV3 determined in lipid nanodisc
Method: EM (single particle) / Resolution: 3.1 Å

20918

6uw6

EMDB-20918, PDB-6uw6:
Cryo-EM structure of the human TRPV3 K169A mutant determined in lipid nanodisc
Method: EM (single particle) / Resolution: 3.66 Å

20919

6uw8

EMDB-20919, PDB-6uw8:
Cryo-EM structure of the human TRPV3 K169A mutant briefly exposed to 2-APB for 3 minutes, determined in lipid nanodisc
Method: EM (single particle) / Resolution: 4.02 Å

20920

6uw9

EMDB-20920, PDB-6uw9:
Cryo-EM structure of the human TRPV3 K169A mutant in the presence of 2-APB, determined in lipid nanodisc
Method: EM (single particle) / Resolution: 4.33 Å

Chemicals

ChemComp-6OU:
[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate / phospholipid*YM

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ion channel / TRPV3 / ion channel TRPV3

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