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J. Biol. Chem., Vol. 279, Issue 45, 46851-46857, November 5, 2004

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High Resolution Studies of the Afa/Dr Adhesin DraE and Its Interaction with Chloramphenicol^*

David Pettigrew, Kirstine L. Anderson¶||, Jason Billington, Ernesto Cota¶||, Peter Simpson¶||, Petri Urvil**, Filip Rabuzin¶||, Pietro Roversi, Bogdan Nowicki**, Laurence du Merle, Chantal Le Bouguénec, Stephen Matthews¶||, and Susan M. Lea

From the Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom, ^¶Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom, ^||Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom, ^**Department of Obstetrics and Gynaecology and Department of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, Texas 77555-1062, and Unite de Pathogénie Bactérienne des Muqueuses, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris CEDEX 15, France

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.

Received for publication, August 13, 2004

^* This work is supported by The Wellcome Trust research leave award (to S. M.), British Biotechnology Science Research Council Grant 43/B16601 (to S. M. L.), Arthritis Research Campaign Grant L0534 (to S. M. L.), Medical Research Council studentship (to D. P.), and an Engineering and Physical Sciences Research Council studentship (to K .L. A.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (codes 1USQ, 1USZ, 1UT1, and 1UT2) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

These authors contributed equally to this work.

To whom correspondence may be addressed. E-mail: s.j.matthews{at}imperial.ac.uk. To whom correspondence may be addressed. E-mail: susan{at}biop.ox.ac.uk.

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