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

Robert M. Stroud; David Savage; Larry J.W. Miercke; John K. Lee; Shahram Khademi; William Harries

doi:10.1016/S0014-5793(03)01195-5

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

Robert M. Stroud, David Savage, Larry J.W. Miercke, John K. Lee, Shahram Khademi, William Harries

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	79-84
Number of pages	6
Journal	FEBS Letters
Volume	555
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(03)01195-5
State	Published - Nov 27 2003

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health (GM24485) to R.M.S.

Keywords

Aquaporin
Channel
Glycerol
Transmembrane
Water

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10.1016/S0014-5793(03)01195-5

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abstract = "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 {\AA} long channel in AqpZ. The basis for absolute exclusion of proton or hydronium ion conductance through the line of water is explored using simulations.",

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AU - Stroud, Robert M.

AU - Savage, David

AU - Miercke, Larry J.W.

AU - Lee, John K.

AU - Khademi, Shahram

AU - Harries, William

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KW - Glycerol

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KW - Water

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