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- W1964937112 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." @default.
- W1964937112 created "2016-06-24" @default.
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- W1964937112 date "2013-09-28" @default.
- W1964937112 modified "2023-10-16" @default.
- W1964937112 title "Purification, crystallization and preliminary X-ray crystallographic analysis of the transport unit of the monomeric autotransporter AIDA-I from<i>Escherichia coli</i>" @default.
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- W1964937112 doi "https://doi.org/10.1107/s1744309113024366" @default.
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