Open AccessPurification, crystallization and preliminary X‐ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA‐I from Escherichia coli
Author(s) -
Gawarzewski Iris,
Tschapek Britta,
Hoeppner Astrid,
Jose Joachim,
Smits Sander H. J.,
Schmitt Lutz
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113024366
Subject(s) - escherichia coli , bacterial outer membrane , bacterial adhesin , crystallization , crystallography , monomer , transport protein , chemistry , membrane , biophysics , biochemistry , biology , polymer , organic chemistry , gene
The adhesin involved in diffuse adherence (AIDA‐I) from Escherichia coli belongs to the group of autotransporters, specifically the type Va secretion system (T5aSS). All autotransporter systems contain a C‐terminal β‐domain, which forms a barrel‐like structure in the outer membrane with a hydrophilic pore allowing passenger translocation across the outer membrane. The passenger domain harbours the biological activity in the extracellular space and functions, for example, as an adhesin, an enzyme and a toxin. The exact transport mechanism of passenger translocation across the outer membrane is not clear at present. Thus, structure determination of the transport unit of AIDA‐I could provide new insights into the transport mechanism. Here, the purification, crystallization and preliminary X‐ray crystallographic studies of the transport unit of AIDA‐I are reported.