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J. Biol. Chem., Vol. 279, Issue 41, 42924-42928, October 8, 2004

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Crystal Structure and Biological Implications of a Bacterial Albumin Binding Module in Complex with Human Serum Albumin^*

Sara Lejon, Inga-Maria Frick¶, Lars Björck¶, Mats Wikström||, and Stefan Svensson||

From the Department of Cell and Molecular Biology, Uppsala University, SE-751 24 Uppsala, Sweden, the ^¶Department of Cell and Molecular Biology, Section for Molecular Pathogenesis, University of Lund, SE-221 00 Lund, Sweden, and the ^||Department of Structural Chemistry, Biovitrum, SE-112 76 Stockholm, Sweden

Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna (formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 Å and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were found to be involved in HSA binding. Furthermore, the presence of HSA-bound fatty acids seems to influence HSA-GA complex formation. F. magna has a much more restricted host specificity compared with C and G streptococci, which is also reflected in the binding of different animal albumins by proteins PAB and G. The structure of the HSA-GA complex offers a molecular explanation to this unusually clear example of bacterial adaptation.

Received for publication, June 22, 2004 , and in revised form, July 20, 2004.

The atomic coordinates and structure factors (code 1TF0) 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 the Swedish Research Council Project Grants 7480 and 14379 and the Foundations of Crafoord and Österlund. 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.

To whom correspondence should be addressed. Tel.: 46-18-4714451; Fax: 46-18-511755; E-mail: sara{at}xray.bmc.uu.se.

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