Structure and selectivity in bestrophin ion channels

Yang, Tingting; Liu, Qun; Kloss, Brian; Bruni, Renato; Kalathur, Ravi C.; Guo, Youzhong; Kloppmann, Edda; Rost, Burkhard; Colecraft, Henry M.; Hendrickson, Wayne A.

doi:10.1126/science.1259723

Title: Structure and selectivity in bestrophin ion channels

Journal Article · Thu Sep 25 00:00:00 EDT 2014 · Science

DOI:https://doi.org/10.1126/science.1259723· OSTI ID:1165950

Yang, Tingting ^[1]; Liu, Qun ^[2]; Kloss, Brian ^[3]; Bruni, Renato ^[3]; Kalathur, Ravi C. ^[3]; Guo, Youzhong ^[1]; Kloppmann, Edda ^[4]; Rost, Burkhard ^[4]; Colecraft, Henry M. ^[5]; Hendrickson, Wayne A. ^[6]

Columbia Univ., New York, NY (United States). Dept. of Biochemistry and Molecular Biophysics
Brookhaven National Lab. (BNL), Upton, NY (United States). New York Structural Biology Center, Synchrotron Beamlines
New York Structural Biology Center, New York, NY (United States). New York Consortium on Membrane Protein Structure (NYCOMPS)
Technische Univ. Munchen, Garching (Germany). Dept. of Informatics, Bioinformatics and Computational Biology
Columbia Univ., New York, NY (United States). Dept. of Physiology and Cellular Biophysics
Columbia Univ., New York, NY (United States). Dept. of Biochemistry and Molecular Biophysics; Brookhaven National Lab. (BNL), Upton, NY (United States). New York Structural Biology Center, Synchrotron Beamlines; New York Structural Biology Center, New York, NY (United States). New York Consortium on Membrane Protein Structure (NYCOMPS); Columbia Univ., New York, NY (United States). Dept. of Physiology and Cellular Biophysics

Human bestrophin 1 (hBest1) is a calcium-activated chloride channel from the retinal pigment epithelium, where it can suffer mutations associated with vitelliform macular degeneration, or Best disease. We describe the structure of a bacterial homolog (KpBest) of hBest1 and functional characterizations of both channels. KpBest is a pentamer that forms a five-helix transmembrane pore, closed by three rings of conserved hydrophobic residues, and has a cytoplasmic cavern with a restricted exit. From electrophysiological analysis of structure-inspired mutations in KpBest and hBest1, we find a subtle control of ion selectivity in the bestrophins, including reversal of anion/cation selectivity, and dramatic activation by mutations at the exit restriction. Lastly, a homology model of hBest1 shows the locations of disease-causing mutations and suggests possible roles in regulation.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE; National Institutes of Health (NIH)

Grant/Contract Number:: AC02-98CH10886; GM095315; GM107462

OSTI ID:: 1165950

Report Number(s):: BNL-107097-2014-JA; R&D Project: LS001

Journal Information:: Science, Vol. 346, Issue 6207; ISSN 0036-8075

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 89 works

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References (44)

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36 MATERIALS SCIENCE
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Crystal structure
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Single-wavelength anomalous diffraction (SAD)
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Title: Structure and selectivity in bestrophin ion channels

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