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Crystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coliCrystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coli
Structural highlights
FunctionAIDA_ECOLX Potent bacterial adhesin that mediates bacterial attachment to a broad variety of human and other mammalian cells. AIDA possesses additional virulence properties, as it is capable of mediating bacterial autoaggregation via intercellular self-recognition and it is a highly efficient initiator of biofilm formation.[1] Publication Abstract from PubMedSeveral serious gastrointestinal diseases, which are widespread all over the world, are caused by enteropathogenic Escherichia coli. The monomeric autotransporter AIDA-I (adhesin involved in diffuse adherence) represents an important virulence factor of these strains and is involved in adhesion, biofilm formation, aggregation and invasion into host cells. Here, we present the crystal structure of the transport unit of AIDA-I at 3.0A resolution, which forms a 12-stranded beta-barrel harboring the linker domain in its pore. Mutagenesis studies of the C-terminal amino acid demonstrated the great impact of this terminal residue on membrane integration of AIDA-I and passenger translocation. Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli.,Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SH, Jose J, Schmitt L J Struct Biol. 2014 May 16. pii: S1047-8477(14)00109-9. doi:, 10.1016/j.jsb.2014.05.003. PMID:24841284[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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