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Science· 2012Q1

Crystal Structure of the Calcium Release–Activated Calcium Channel Orai

Xiaowei Hou, Leanne Pedi, Melinda M. Diver, Stephen B. Long

Short summary

The crystal structure of the Drosophila melanogaster Orai protein reveals a hexameric assembly forming a central ion pore, with a glutamate ring acting as the selectivity filter and a basic region potentially stabilizing the closed state.

AI-generated from the title and abstract; the full text is not read.

Key points

  • Orai forms a hexameric assembly with a central ion pore.
  • The pore traverses the membrane and extends into the cytosol.
  • A ring of extracellular glutamate residues acts as the selectivity filter.
  • An intracellular basic region may stabilize the closed state by binding anions.

AI-generated from the title and abstract; the full text is not read.

Abstract

The plasma membrane protein Orai forms the pore of the calcium release-activated calcium (CRAC) channel and generates sustained cytosolic calcium signals when triggered by depletion of calcium from the endoplasmic reticulum. The crystal structure of Orai from Drosophila melanogaster, determined at 3.35 angstrom resolution, reveals that the calcium channel is composed of a hexameric assembly of Orai subunits arranged around a central ion pore. The pore traverses the membrane and extends into the cytosol. A ring of glutamate residues on its extracellular side forms the selectivity filter. A basic region near the intracellular side can bind anions that may stabilize the closed state. The architecture of the channel differs markedly from other ion channels and gives insight into the principles of selective calcium permeation and gating.

The authors' abstract, as published at the source. Science, 2012 · DOI ↗

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Field: Sensory Systems

Sensory SystemsNeuroscience