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Selectivity for maltose and maltodextrins of maltoporin, a pore‐forming protein of E. coli outer membrane
Author(s) -
Dargent Bénédicte,
Rosenbusch Jürg,
Pattus Franc
Publication year - 1987
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 - 10.1016/0014-5793(87)80891-8
Subject(s) - maltose , chemistry , selectivity , porin , membrane , bacterial outer membrane , biophysics , escherichia coli , biochemistry , biology , sucrose , gene , catalysis
Homogeneous maltoporin (lamB protein), an Escherichia coli outer membrane spanning protein, was incorporated in phospholipid planar bilayers. It generates aqueous channels distinct from those formed by the non‐specific porin (OmpF) or by phosphoporin (phoE protein). The single conductance, 150 pS in 1 M NACl, is much smaller than that of the porins. The channels, which are poorly selective for cations and voltage independent, are specifically inhibited by maltose and maltodextrins. This inhibition, observed in the absence of maltose binding protein, demonstrates that the selectivity of maltoporin for maltose and maltodextrins is an intrinsic property of the protein.