Literature DB >> 2440722

Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E. coli outer membrane.

B Dargent, J Rosenbusch, F Pattus.   

Abstract

Homogenous 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.

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Year:  1987        PMID: 2440722     DOI: 10.1016/0014-5793(87)80891-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  9 in total

1.  Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from Escherichia coli.

Authors:  K Gehring; C H Cheng; H Nikaido; B K Jap
Journal:  J Bacteriol       Date:  1991-03       Impact factor: 3.490

2.  Transport of maltodextrins through maltoporin: a single-channel study.

Authors:  Lisen Kullman; Mathias Winterhalter; Sergey M Bezrukov
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

3.  Computer simulations of the OmpF porin from the outer membrane of Escherichia coli.

Authors:  M Watanabe; J Rosenbusch; T Schirmer; M Karplus
Journal:  Biophys J       Date:  1997-05       Impact factor: 4.033

4.  The Salmonella enterica serovar Typhi tsx gene, encoding a nucleoside-specific porin, is essential for prototrophic growth in the absence of nucleosides.

Authors:  Sergio A Bucarey; Nicolás A Villagra; Mara P Martinic; A Nicole Trombert; Carlos A Santiviago; Nancy P Maulén; Philip Youderian; Guido C Mora
Journal:  Infect Immun       Date:  2005-10       Impact factor: 3.441

5.  The major outer membrane protein of Acidovorax delafieldii is an anion-selective porin.

Authors:  M Brunen; H Engelhardt; A Schmid; R Benz
Journal:  J Bacteriol       Date:  1991-07       Impact factor: 3.490

6.  Structural basis for outer membrane sugar uptake in pseudomonads.

Authors:  Bert van den Berg
Journal:  J Biol Chem       Date:  2012-10-12       Impact factor: 5.157

7.  Noise analysis of ion current through the open and the sugar-induced closed state of the LamB channel of Escherichia coli outer membrane: evaluation of the sugar binding kinetics to the channel interior.

Authors:  S Nekolla; C Andersen; R Benz
Journal:  Biophys J       Date:  1994-05       Impact factor: 4.033

8.  Three-dimensional reconstruction of maltoporin from electron microscopy and image processing.

Authors:  J Lepault; B Dargent; W Tichelaar; J P Rosenbusch; K Leonard; F Pattus
Journal:  EMBO J       Date:  1988-01       Impact factor: 11.598

9.  Evaluation of the rate constants of sugar transport through maltoporin (LamB) of Escherichia coli from the sugar-induced current noise.

Authors:  C Andersen; M Jordy; R Benz
Journal:  J Gen Physiol       Date:  1995-03       Impact factor: 4.086

  9 in total

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