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J. Biol. Chem., Vol. 280, Issue 17, 17339-17345, April 29, 2005

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Crystal Structure of Hemoglobin Protease, a Heme Binding Autotransporter Protein from Pathogenic Escherichia coli^*

Ben R. Otto, Robert Sijbrandi, Joen Luirink, Bauke Oudega, Jonathan G. Heddle, Kenji Mizutani, Sam-Yong Park, and Jeremy R. H. Tame¶

From the Department of Molecular Microbiology, Faculty of Earth and Life Sciences, Vrije Universiteit de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands and the Protein Design Laboratory, Yokohama City University, Suehiro-cho 1-7-29, Tsurumi, Yokohama 230-0045, Japan

The acquisition of iron is essential for the survival of pathogenic bacteria, which have consequently evolved a wide variety of uptake systems to extract iron and heme from host proteins such as hemoglobin. Hemoglobin protease (Hbp) was discovered as a factor involved in the symbiosis of pathogenic Escherichia coli and Bacteroides fragilis, which cause intra-abdominal abscesses. Released from E. coli, this serine protease autotransporter degrades hemoglobin and delivers heme to both bacterial species. The crystal structure of the complete passenger domain of Hbp (110 kDa) is presented, which is the first structure from this class of serine proteases and the largest parallel -helical structure yet solved.

Received for publication, November 15, 2004 , and in revised form, February 17, 2005.

^* 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 (code 1WXR) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^¶ To whom correspondence should be addressed. Tel.: 81-(0)45-508-7228; Fax: 81-(0)45-508-7366; E-mail: jtame{at}tsurumi.yokohamacu.ac.jp.

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