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  Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus

Wang, T., Langer, J. D., Peng, G., & Michel, H. (2012). Isolation, functional characterization and crystallization of Aq_1259, an outer membrane protein with porin features, from Aquifex aeolicus. Biochimica et Biophysica Acta-Proteins and Proteomics, 1824(12), 1358-1365. doi:10.1016/j.bbapap.2012.07.004.

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 Creators:
Wang, Tao1, Author              
Langer, Julian David1, Author              
Peng, Guohong1, 2, Author              
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China, ou_persistent22              

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Free keywords: Aq_1259; Porin; Aquifex aeolicus; Hypothetical protein
 Abstract: The “hypothetical protein” Aq_1259 was identified by mass spectrometry and purified from native membranes of Aquifex aeolicus. It is a 49.4 kDa protein, highly homologous (>52% identity) to several conserved hypothetical proteins from other bacteria. However, none of these proteins has been characterized using biochemical or electrophysiological techniques. Based on the sequence and circular dichroism spectroscopy, the structure of Aq_1259 is predicted to be a β-barrel with 16 β-strands. The strands with loops and turns are distributed evenly through the entire sequence. The function of Aq_1259 was analyzed after incorporation into a lipid bilayer. Electrophysiological measurements revealed a pore that has a basic stationary conductance of 0.48±0.038 nS in a buffer with 0.5 M NaH2PO4 at pH 6.5 and 0.2±0.015 nS in a buffer with 0.5 M NaCl at pH 6.5. Superimposed on this is a fluctuating conductance of similar amplitude. Aq_1259 could be crystallized. The crystals diffract to a resolution of 3.4 Å and belong to space group I222 with cell dimensions of a=138.3 Å, b=144.6 Å, c=151.8 Å.

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Language(s): eng - English
 Dates: 2012-06-222012-03-262012-07-182012-07-242012-12
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbapap.2012.07.004
 Degree: -

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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
  Other : BBA-Proteins Proteomics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1824 (12) Sequence Number: - Start / End Page: 1358 - 1365 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5