4MEE
Crystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coli
Summary for 4MEE
| Entry DOI | 10.2210/pdb4mee/pdb |
| Descriptor | Diffuse adherence adhesin (1 entity in total) |
| Functional Keywords | beta barrel, outer membrane protein, autotransporter, protein binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 50952.49 |
| Authors | Gawarzewski, I.,Tschapek, B.,Hoeppner, A.,Smits, S.H.,Jose, J.,Schmitt, L. (deposition date: 2013-08-26, release date: 2014-06-04, Last modification date: 2024-02-28) |
| Primary citation | Gawarzewski, I.,DiMaio, F.,Winterer, E.,Tschapek, B.,Smits, S.H.,Jose, J.,Schmitt, L. Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J.Struct.Biol., 187:20-29, 2014 Cited by PubMed Abstract: 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 3.0Å resolution, which forms a 12-stranded β-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. PubMed: 24841284DOI: 10.1016/j.jsb.2014.05.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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