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Structure paper

TitleStructures of the TRPM5 channel elucidate mechanisms of activation and inhibition.
Journal, issue, pagesNat Struct Mol Biol, Vol. 28, Issue 7, Page 604-613, Year 2021
Publish dateJun 24, 2021
AuthorsZheng Ruan / Emery Haley / Ian J Orozco / Mark Sabat / Richard Myers / Rebecca Roth / Juan Du / Wei Lü /
PubMed AbstractThe Ca-activated TRPM5 channel plays essential roles in taste perception and insulin secretion. However, the mechanism by which Ca regulates TRPM5 activity remains elusive. We report cryo-EM ...The Ca-activated TRPM5 channel plays essential roles in taste perception and insulin secretion. However, the mechanism by which Ca regulates TRPM5 activity remains elusive. We report cryo-EM structures of the zebrafish TRPM5 in an apo closed state, a Ca-bound open state, and an antagonist-bound inhibited state. We define two novel ligand binding sites: a Ca site (Ca) in the intracellular domain and an antagonist site in the transmembrane domain (TMD). The Ca site is unique to TRPM5 and has two roles: modulating the voltage dependence and promoting Ca binding to the Ca site, which is conserved throughout TRPM channels. Conformational changes initialized from both Ca sites cooperatively open the ion-conducting pore. The antagonist NDNA wedges into the space between the S1-S4 domain and pore domain, stabilizing the transmembrane domain in an apo-like closed state. Our results lay the foundation for understanding the voltage-dependent TRPM channels and developing new therapeutic agents.
External linksNat Struct Mol Biol / PubMed:34168372 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.6 Å
Structure data

EMDB-23740, PDB-7mbp:
Cryo-EM structure of zebrafish TRPM5 in the presence of 1 mM EDTA
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-23741, PDB-7mbq:
Cryo-EM structure of zebrafish TRPM5 in the presence of 5 mM calcium
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-23742:
Zebrafish TRPM5 with 1 mM EDTA in nanodisc
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-23743:
Zebrafish TRPM5 with 1 mM calcium and 0.5 mM steviol in nanodisc at 3.0 Angstroms resolution
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-23744, PDB-7mbr:
Cryo-EM structure of zebrafish TRPM5 in the presence of 6 uM calcium (apo state)
Method: EM (single particle)

EMDB-23745, PDB-7mbs:
Cryo-EM structure of zebrafish TRPM5 in the presence of 6 uM calcium (open state)
Method: EM (single particle)

EMDB-23746, PDB-7mbt:
Cryo-EM structure of zebrafish TRPM5 E337A mutant in the presence of 5 mM calcium (low calcium occupancy in the transmembrane domain)
Method: EM (single particle)

EMDB-23747, PDB-7mbu:
Cryo-EM structure of zebrafish TRPM5 E337A mutant in the presence of 5 mM calcium (high calcium occupancy in the transmembrane domain)
Method: EM (single particle)

EMDB-23748, PDB-7mbv:
Cryo-EM structure of zebrafish TRPM5 in the presence of 5 mM calcium and 0.5 mM NDNA
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-YUV:
(25R)-14beta,17beta-spirost-5-en-3beta-ol / Diosgenin

ChemComp-YUY:
(2R)-2-(hydroxymethyl)-4-{[(25R)-10alpha,14beta,17beta-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-YUS:
N'-[(E)-(3,4-dimethoxyphenyl)methylidene]-2-(naphthalen-1-yl)acetohydrazide

Source
  • danio rerio (zebrafish)
KeywordsTRANSPORT PROTEIN / Ion channel / TRP channel

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