1RXL

Solution structure of the engineered protein Afae-dsc

Summary for 1RXL

• Entry DOI: 10.2210/pdb1rxl/pdb
• Related: 1SDD 1USQ 1USZ 1UT1 1UT2
• NMR Information: BMRB: 5947
• Descriptor: Afimbrial adhesin AFA-III (1 entity in total)
• Functional Keywords: afae, daf, afimbrial sheath, daec, upec, ig-like domain, donor strand complemented, structural protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 16952.71

Authors

Anderson, K.L.,Billington, J.,Pettigrew, D.,Cota, E.,Roversi, P.,Simpson, P.,Chen, H.A.,Urvil, P.,du Merle, L.,Barlow, P.N.,Medof, M.E.,Smith, R.A.,Nowicki, B.,Le Bouguenec, C.,Lea, S.M.,Matthews, S. (deposition date: 2003-12-18, release date: 2005-01-11, Last modification date: 2020-02-05)

Primary citation

Anderson, K.L.,Billington, J.,Pettigrew, D.,Cota, E.,Simpson, P.,Roversi, P.,Chen, H.A.,Urvil, P.,du Merle, L.,Barlow, P.N.,Medof, M.E.,Smith, R.A.,Nowicki, B.,Le Bouguenec, C.,Lea, S.M.,Matthews, S.
An atomic resolution model for assembly, architecture, and function of the Dr adhesins.
Mol.Cell, 15:647-657, 2004

PubMed Abstract: Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.

PubMed: 15327779
DOI: 10.1016/j.molcel.2004.08.003

Experimental method

SOLUTION NMR