The Structure of Porin from Rhodobacter capsulatus at 6 Å

  • W. Welte
  • T. Wacker
  • U. Nestel
  • D. Woitzik
  • J. Weckesser
  • M. S. Weiss
  • G. E. Schulz
Part of the FEMS Symposium book series (FEMSS)

Abstract

Porins are a class of integral membrane proteins which confer well-defined permeability properties to the outer membrane of gram-negative bacteria. They form aqueous channels across the outer membrane which allow the passage of small polar molecules up to an exclusion size of, typically, 600 daltons. For recent reviews see [1, 2, 3]. The geometry of the channel and the distribution of the amino acid side chains which form its surface, determine the individual characteristics of porins : the exclusion limit as well as the selectivity as e.g. for anions, cations, phosphates or sugars[3, 4]. Except for this selectivity the solutes seem to pass the channel by free diffusion. The exclusion limit is large enough to allow for the passage of antibiotics[5].

Keywords

Outer Membrane Integral Membrane Protein Exclusion Limit Hydrophilic Loop Guanidinium Hydrochloride 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • W. Welte
    • 1
  • T. Wacker
    • 1
  • U. Nestel
    • 1
  • D. Woitzik
    • 2
  • J. Weckesser
    • 2
  • M. S. Weiss
    • 3
  • G. E. Schulz
    • 3
  1. 1.Institut für Biophysik und StrahlenbiologieFreiburg i.Br.Germany
  2. 2.Institut für Biologie II, MikrobiologieFreiburg i.Br.Germany
  3. 3.Institut für Organische Chemie und BiochemieFreiburg i.Br.Germany

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