Structural highlights
Publication Abstract from PubMed
Several 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Gawarzewski I, DiMaio F, Winterer E, Tschapek B, Smits SH, Jose J, Schmitt L. Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J Struct Biol. 2014 May 16. pii: S1047-8477(14)00109-9. doi:, 10.1016/j.jsb.2014.05.003. PMID:24841284 doi:http://dx.doi.org/10.1016/j.jsb.2014.05.003
