Deutsch
 
Benutzerhandbuch Datenschutzhinweis Impressum Kontakt
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Zeitschriftenartikel

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

MPG-Autoren
/persons/resource/persons137938

Wang,  Tao
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Langer,  Julian D.
Max Planck Society;

/persons/resource/persons137832

Peng,  Guohong
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137800

Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

Externe Ressourcen
Es sind keine Externen Ressourcen verfügbar
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

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 (BBA) - Proteins and Proteomics, 1824(12), 1358-1365.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0024-D537-E
Zusammenfassung
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.