crystal structure of a yeast aquaporin at 1.15 ？ reveals a novel gating mechanism晶体结构的酵母水通道蛋白在1.15 揭示了一种新型闸门机制.pdf

˚ Crystal Structure of a Yeast Aquaporin at 1.15 A Reveals a Novel Gating Mechanism 1. 1. ´ 2 3 Gerhard Fischer , Urszula Kosinska-Eriksson , Camilo Aponte-Santamarıa , Madelene Palmgren , 3 1 3 2 1 Cecilia Geijer , Kristina Hedfalk , Stefan Hohmann , Bert L. de Groot , Richard Neutze *, Karin Lindkvist- Petersson3* ¨ 1 Department of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Goteborg, Sweden, 2 Computational Biomolecular Dynamics Group, Max Planck ¨ ¨ Institute for Biophysical Chemistry, Gottingen, Germany, 3 Department of Cell and Molecular Biology, University of Gothenburg, Goteborg, Sweden Abstract Aquaporins are transmembrane proteins that facilitate the flow of water through cellular membranes. An unusual characteristic of yeast aquaporins is that they frequently contain an extended N terminus of unknown function. Here we ˚ present the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A resolution. Our crystal structure reveals that the wa