Report

Water Permeation Across Biological Membranes: Mechanism and Dynamics of Aquaporin-1 and GlpF

Science  14 Dec 2001:
Vol. 294, Issue 5550, pp. 2353-2357
DOI: 10.1126/science.1066115

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


Abstract

“Real time” molecular dynamics simulations of water permeation through human aquaporin-1 (AQP1) and the bacterial glycerol facilitator GlpF are presented. We obtained time-resolved, atomic-resolution models of the permeation mechanism across these highly selective membrane channels. Both proteins act as two-stage filters: Conserved fingerprint [asparagine-proline-alanine (NPA)] motifs form a selectivity-determining region; a second (aromatic/arginine) region is proposed to function as a proton filter. Hydrophobic regions near the NPA motifs are rate-limiting water barriers. In AQP1, a fine-tuned water dipole rotation during passage is essential for water selectivity. In GlpF, a glycerol-mediated “induced fit” gating motion is proposed to generate selectivity for glycerol over water.

  • * To whom correspondence should be addressed. E-mail: hgrubmu{at}gwdg.de

View Full Text

Related Content