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TitleFull-Length P2X Structures Reveal How Palmitoylation Prevents Channel Desensitization.
Journal, issue, pagesCell, Vol. 179, Issue 3, Page 659-670.e13, Year 2019
Publish dateOct 17, 2019
AuthorsAlanna E McCarthy / Craig Yoshioka / Steven E Mansoor /
PubMed AbstractP2X receptors are trimeric, non-selective cation channels activated by extracellular ATP. The P2X receptor subtype is a pharmacological target because of involvement in apoptotic, inflammatory, and ...P2X receptors are trimeric, non-selective cation channels activated by extracellular ATP. The P2X receptor subtype is a pharmacological target because of involvement in apoptotic, inflammatory, and tumor progression pathways. It is the most structurally and functionally distinct P2X subtype, containing a unique cytoplasmic domain critical for the receptor to initiate apoptosis and not undergo desensitization. However, lack of structural information about the cytoplasmic domain has hindered understanding of the molecular mechanisms underlying these processes. We report cryoelectron microscopy structures of full-length rat P2X receptor in apo and ATP-bound states. These structures reveal how one cytoplasmic element, the C-cys anchor, prevents desensitization by anchoring the pore-lining helix to the membrane with palmitoyl groups. They show a second cytoplasmic element with a unique fold, the cytoplasmic ballast, which unexpectedly contains a zinc ion complex and a guanosine nucleotide binding site. Our structures provide first insights into the architecture and function of a P2X receptor cytoplasmic domain.
External linksCell / PubMed:31587896 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.3 Å
Structure data

20702

6u9v

EMDB-20702: EMDB: Cryo electron microscopy map of the ATP-gated rat P2X7 ion channel in the apo, closed state
PDB-6u9v: Cryo electron microscopy structure of the ATP-gated rat P2X7 ion channel in the apo, closed state
Method: EM (single particle) / Resolution: 2.9 Å

20703

6u9w

EMDB-20703: Cryo electron microscopy map of the ATP-gated rat P2X7 ion channel in the ATP-bound, open state
PDB-6u9w: Cryo electron microscopy structure of the ATP-gated rat P2X7 ion channel in the ATP-bound, open state
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-Q3G:
O-[(R)-[(2S)-2-(hexadecanoyloxy)-3-(octadecanoyloxy)propoxy](hydroxy)phosphoryl]-D-serine / phospholipid*YM

ChemComp-PLM:
PALMITIC ACID

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / Ion Channel Apoptosis

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