1UT1

DraE adhesin from Escherichia Coli

Summary for 1UT1

• Entry DOI: 10.2210/pdb1ut1/pdb
• Related: 1USQ 1USZ 1UT2
• Descriptor: DR HEMAGGLUTININ STRUCTURAL SUBUNIT, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: adhesin, protein binding fimbrial adhesin, upec, daec, protein binding
• Biological source: ESCHERICHIA COLI
• Cellular location: Fimbrium: P24093
• Total number of polymer chains: 6
• Total formula weight: 99511.39

Authors

Anderson, K.L.,Billington, J.,Pettigrew, D.,Cota, E.,Roversi, P.,Simpson, P.,Chen, H.A.,Urvil, P.,Dumerle, L.,Barlow, P.,Medof, E.,Smith, R.A.G.,Nowicki, B.,Le Bouguenec, C.,Lea, S.M.,Matthews, S. (deposition date: 2003-12-02, release date: 2004-08-31, Last modification date: 2024-11-20)

Primary citation

Pettigrew, D.,Anderson, K.L.,Billington, J.,Cota, E.,Simpson, P.,Urvil, P.,Rabuzin, F.,Roversi, P.,Nowicki, B.,Du Merle, L.,Le Bouguenec, C.,Matthews, S.,Lea, S.M.
High Resolution Studies of the Afa/Dr Adhesin Drae and its Interaction with Chloramphenicol
J.Biol.Chem., 279:46851-, 2004

PubMed Abstract: Pathogenic Escherichia coli expressing Afa/Dr adhesins are able to cause both urinary tract and diarrheal infections. The Afa/Dr adhesins confer adherence to epithelial cells via interactions with the human complement regulating protein, decay accelerating factor (DAF or CD55). Two of the Afa/Dr adhesions, AfaE-III and DraE, differ from each other by only three residues but are reported to have several different properties. One such difference is disruption of the interaction between DraE and CD55 by chloramphenicol, whereas binding of AfaE-III to CD55 is unaffected. Here we present a crystal structure of a strand-swapped trimer of wild type DraE. We also present a crystal structure of this trimer in complex with chloramphenicol, as well as NMR data supporting the binding position of chloramphenicol within the crystal. The crystal structure reveals the precise atomic basis for the sensitivity of DraE-CD55 binding to chloramphenicol and demonstrates that in contrast to other chloramphenicol-protein complexes, drug binding is mediated via recognition of the chlorine "tail" rather than via intercalation of the benzene rings into a hydrophobic pocket.

PubMed: 15331605
DOI: 10.1074/JBC.M409284200

Experimental method

X-RAY DIFFRACTION (1.7 Å)