Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins

Peter Nollert, William E.C. Harries, Daxiong Fu, Larry J.W. Miercke, Robert M. Stroud

Research output: Contribution to journalShort survey

Abstract

The structure of a glycerol channel from Escherichia coli at 2.2 Å resolution serves as a basis for the understanding of selective transmembrane substrate permeation. In the course of permeation, glycerol molecules diffuse through a tripathic channel with their alkyl backbone wedged against a hydrophobic corner, such that OH groups become acceptors and donors of hydrogen bonds at the same time. The structure of the channel explains the preferential permeability for linear carbohydrates and absolute exclusion of ions and charged solutes. Its gene-duplicated sequence has a structural counterpart in a pseudo two-fold symmetry within the monomeric channel protein.

Original languageEnglish (US)
Pages (from-to)112-117
Number of pages6
JournalFEBS Letters
Volume504
Issue number3
DOIs
StatePublished - Aug 31 2001
Externally publishedYes

Keywords

  • Aquaglyceroporin
  • Aquaporin
  • Channel
  • Glycerol
  • Membrane permeation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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