Selectivity and conductance among the glycerol and water conducting aquaporin family of channels

FEBS Letters

Harries, William¹  Lee, John K.¹  Khademi, Shahram¹  Savage, David¹  Stroud, Robert M.¹  Miercke, Larry J.W.¹ 

[1] Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-2240, USA

关键词: Channel;    Transmembrane;    Glycerol;    Water;    Aquaporin;    GlpF;    glycerol channel from E. coli;    AqpZ;    aquaporin Z from E. coli;    AQPs;    family of water conducting aquaporins and glycerol plus water conducting aquaglyceroporins;   

DOI  :  10.1016/S0014-5793(03)01195-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The atomic structures of a transmembrane water plus glycerol conducting channel (GlpF), and now of aquaporin Z (AqpZ) from the same species, Escherichia coli, bring the total to three atomic resolution structures in the aquaporin (AQP) family. Members of the AQP family each assemble as tetramers of four channels. Common helical axes support a wider channel in the glycerol plus water channel paradigm, GlpF. Water molecules form a single hydrogen bonded file throughout the 28 Å long channel in AqpZ. The basis for absolute exclusion of proton or hydronium ion conductance through the line of water is explored using simulations.

【 授权许可】

Unknown