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  Projection structure of the monomeric porin OmpG at 6 å resolution

Behlau, M., Mills, D. J., Quader, H., Kühlbrandt, W., & Vonck, J. (2001). Projection structure of the monomeric porin OmpG at 6 å resolution. Journal of Molecular Biology (London), 305(1), 71-77. doi:10.1006/jmbi.2000.4284.

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 Creators:
Behlau, Matthias1, Author
Mills, Deryck J.2, Author                 
Quader, Hartmut1, Author
Kühlbrandt, Werner2, Author                 
Vonck, Janet2, Author                 
Affiliations:
1Institut für Allgemeine Botanik und Botanischer Garten, Ohnhorststrasse 18 D-22609, Hamburg, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: electron crystallography; 2-D crystals; membrane protein; porin; β-barrel
 Abstract: The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and trisaccharides, has been purified and crystallized in two dimensions. Projection maps of two different crystal forms of OmpG at 6 Å resolution show that the protein has a β-barrel structure characteristic for outer membrane proteins, and that it does not form trimers, unlike most other porins such as OmpF and OmpC, but appears in monomeric form. The size of the barrel is ∼2.5 nm, indicating that OmpG may consist of 14 β-strands. The projection map suggests that the channel is restricted by internal loops.

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Language(s): eng - English
 Dates: 2000-10-252000-07-202000-10-302002-05-252001-01-05
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1006/jmbi.2000.4284
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 305 (1) Sequence Number: - Start / End Page: 71 - 77 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042