1ut1

From Proteopedia

Revision as of 09:12, 30 October 2007

DRAE ADHESIN FROM ESCHERICHIA COLI

Overview

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 ... [(full description)]

About this Structure

1UT1 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 and EDO as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol., Pettigrew D, Anderson KL, Billington J, Cota E, Simpson P, Urvil P, Rabuzin F, Roversi P, Nowicki B, du Merle L, Le Bouguenec C, Matthews S, Lea SM, J Biol Chem. 2004 Nov 5;279(45):46851-7. Epub 2004 Aug 24. PMID:15331605

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