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J. Biol. Chem., Vol. 278, Issue 42, 41093-41098, October 17, 2003

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Crystal Structure of Pasteurella haemolytica Ferric Ion-binding Protein A Reveals a Novel Class of Bacterial Iron-binding Proteins^*

Stephen R. Shouldice  , Douglas R. Dougan  ¶, Pamela A. Williams ||, Robert J. Skene ¶, Gyorgy Snell ¶, Daniel Scheibe ¶, Shane Kirby , David J. Hosfield ¶, Duncan E. McRee ¶, Anthony B. Schryvers  and Leslie W. Tari ¶ **

From the Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta T2N 4N1, Canada, ^¶Syrrx, Inc., San Diego, California, 92121, and ^||Astex Technology, Cambridge CB4 0QA, United Kingdom

Pasteurellosis caused by the Gram-negative pathogen Pasteurella haemolytica is a serious disease leading to death in cattle. To scavenge growth-limiting iron from the host, the pathogen utilizes the periplasmic ferric ion-binding protein A (PhFbpA) as a component of an ATP-binding cassette transport pathway. We report the 1.2-Å structure of the iron-free (apo) form of PhFbpA, which is a member of the transferrin structural superfamily. The protein structure adopts a closed conformation, allowing us to reliably assign putative iron-coordinating residues. Based on our analysis, PhFbpA utilizes a unique constellation of binding site residues and anions to octahedrally coordinate an iron atom. A surprising finding in the structure is the presence of two formate anions on opposite sides of the iron-binding pocket. The formate ions tether the N- and C-terminal domains of the protein and stabilize the closed structure, also providing clues as to probable candidates for synergistic anions in the iron-loaded state. PhFbpA represents a new class of bacterial iron-binding proteins.

Received for publication, June 26, 2003 , and in revised form, July 25, 2003.

The atomic coordinates and structure factors (code 1Q35) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by Grant 49603 from the Canadian Institutes for Health Research. This work is based on diffraction experiments conducted at the ALS. 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.

Both authors contributed equally to this work.

^** To whom correspondence should be addressed: Associate Director, Crystallography, Syrrx Inc., 10410 Science Center Dr., San Diego, CA, 92121. Tel.: 858-622-8528 (ext. 3624); Fax: 858-550-0598; E-mail: ltari{at}syrrx.com.

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