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

FEBS Lett. 2003 Nov 27;555(1):79-84. doi: 10.1016/s0014-5793(03)01195-5.

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.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Aquaporin 1
  • Aquaporins / chemistry*
  • Aquaporins / genetics
  • Aquaporins / metabolism
  • Carbohydrate Metabolism
  • Electric Conductivity
  • Electrochemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Gene Duplication
  • Glycerol / metabolism
  • Membrane Proteins*
  • Models, Molecular
  • Molecular Sequence Data
  • Potassium Channels / chemistry
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Water / metabolism

Substances

  • Aquaporins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Potassium Channels
  • aqpZ protein, E coli
  • Water
  • GlpF protein, E coli
  • Aquaporin 1
  • Glycerol