Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|69|10|1159-1162
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.69, Iss.10, 2013-10, pp. : 1159-1162
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Abstract
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.
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