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

被引：53

作者：

Stroud, RM ^{[1
]}

Savage, D ^{[1
]}

Miercke, LJW ^{[1
]}

Lee, JK ^{[1
]}

Khademi, S ^{[1
]}

Harries, W ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA

来源：

FEBS LETTERS | 2003年 / 555卷 / 01期

关键词：

channel; transmembrane; glycerol; water; aquaporin;

D O I：

10.1016/S0014-5793(03)01195-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The atomic structures of a transmembrane water plus glycerol conducting channel (GIpF), 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, GIpF. Water molecules form a single hydrogen bonded file throughout the 28 long channel in AqpZ. The basis for absolute exclusion of proton or hydronium ion conductance through the line of water is explored using simulations. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：79 / 84

页数：6

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