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Atomic structure of a glycerol channel and implications for substrate permeation in aqua(glycero)porins
Author(s) -
Nollert Peter,
Harries William E.C,
Fu Daxiong,
Miercke Larry J.W,
Stroud Robert M
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02710-7
Subject(s) - permeation , glycerol , chemistry , monomer , membrane , alkyl , hydrogen bond , molecule , substrate (aquarium) , crystallography , transmembrane protein , organic chemistry , biochemistry , polymer , oceanography , receptor , geology
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.