Format

Send to

Choose Destination
FEBS Lett. 2003 Nov 27;555(1):79-84.

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

Author information

1
Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-2240, USA. stroud@msg.ucsf.edu

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 A long channel in AqpZ. The basis for absolute exclusion of proton or hydronium ion conductance through the line of water is explored using simulations.

PMID:
14630323
DOI:
10.1016/s0014-5793(03)01195-5
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center