Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins

FEBS Letters

Harries, William E.C¹  Nollert, Peter¹  Stroud, Robert M¹  Miercke, Larry J.W¹  Fu, Daxiong¹ 

[1]Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco, CA 94143-0448, USA

关键词: Aquaporin;    Aquaglyceroporin;    Glycerol;    Channel;    Membrane permeation;    GlpF;    the glycerol channel from Escherichia coli;    AQPs;    aquaporins;   

DOI  :  10.1016/S0014-5793(01)02710-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of a glycerol channel from Escherichia coli at 2.2 Å resolution serves as a basis for the understanding of selective transmembrane substrate permeation. In the course of permeation, glycerol molecules diffuse through a tripathic channel with their alkyl backbone wedged against a hydrophobic corner, such that OH groups become acceptors and donors of hydrogen bonds at the same time. The structure of the channel explains the preferential permeability for linear carbohydrates and absolute exclusion of ions and charged solutes. Its gene-duplicated sequence has a structural counterpart in a pseudo two-fold symmetry within the monomeric channel protein.

【 授权许可】

Unknown