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

Access

10.1016/S0014-5793(03)01195-5

Cite this

@article{b4da16b806194e6d8a231eb3ed47e104,

title = "Selectivity and conductance among the glycerol and water conducting aquaporin family of channels",

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.",

keywords = "Aquaporin, Channel, Glycerol, Transmembrane, Water",

author = "Stroud, {Robert M.} and David Savage and Miercke, {Larry J.W.} and Lee, {John K.} and Shahram Khademi and William Harries",

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

year = "2003",

month = nov,

day = "27",

doi = "10.1016/S0014-5793(03)01195-5",

language = "English (US)",

volume = "555",

pages = "79--84",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Selectivity and conductance among the glycerol and water conducting aquaporin family of channels

AU - Stroud, Robert M.

AU - Savage, David

AU - Miercke, Larry J.W.

AU - Lee, John K.

AU - Khademi, Shahram

AU - Harries, William

N1 - Funding Information: This work was supported by the National Institutes of Health (GM24485) to R.M.S.

PY - 2003/11/27

Y1 - 2003/11/27

N2 - 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.

AB - 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.

KW - Aquaporin

KW - Channel

KW - Glycerol

KW - Transmembrane

KW - Water

UR - http://www.scopus.com/inward/record.url?scp=0242405520&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242405520&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(03)01195-5

DO - 10.1016/S0014-5793(03)01195-5

M3 - Article

C2 - 14630323

AN - SCOPUS:0242405520

VL - 555

SP - 79

EP - 84

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -

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

Abstract

Bibliographical note

Keywords

Access

Other files and links

Fingerprint

Cite this