5F1C

Crystal structure of an invertebrate P2X receptor from the Gulf Coast tick in the presence of ATP and Zn2+ ion at 2.9 Angstroms

Summary for 5F1C

• Entry DOI: 10.2210/pdb5f1c/pdb
• Descriptor: Putative uncharacterized protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
• Functional Keywords: ligand, complex, channel, agonist, membrane protein
• Biological source: Amblyomma maculatum (Gulf Coast tick)
• Total number of polymer chains: 3
• Total formula weight: 124030.09

Authors

Kasuya, G.,Hattori, M.,Ishitani, R.,Nureki, O. (deposition date: 2015-11-30, release date: 2016-03-16, Last modification date: 2024-10-30)

Primary citation

Kasuya, G.,Fujiwara, Y.,Takemoto, M.,Dohmae, N.,Nakada-Nakura, Y.,Ishitani, R.,Hattori, M.,Nureki, O.
Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels
Cell Rep, 14:932-944, 2016

PubMed Abstract: P2X receptors are trimeric ATP-gated cation channels involved in physiological processes ranging widely from neurotransmission to pain and taste signal transduction. The modulation of the channel gating, including that by divalent cations, contributes to these diverse physiological functions of P2X receptors. Here, we report the crystal structure of an invertebrate P2X receptor from the Gulf Coast tick Amblyomma maculatum in the presence of ATP and Zn(2+) ion, together with electrophysiological and computational analyses. The structure revealed two distinct metal binding sites, M1 and M2, in the extracellular region. The M1 site, located at the trimer interface, is responsible for Zn(2+) potentiation by facilitating the structural change of the extracellular domain for pore opening. In contrast, the M2 site, coupled with the ATP binding site, might contribute to regulation by Mg(2+). Overall, our work provides structural insights into the divalent cation modulations of P2X receptors.

PubMed: 26804916
DOI: 10.1016/j.celrep.2015.12.087

Experimental method

X-RAY DIFFRACTION (2.9 Å)