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Originally published In Press as doi:10.1074/jbc.M109943200 on December 18, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8114-8120, March 8, 2002
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Structure, Specificity, and Mode of Interaction for Bacterial Albumin-binding Modules*

Maria U. JohanssonDagger §, Inga-Maria Frick, Hanna NilssonDagger , Per J. Kraulis||**, Sophia HoberDagger Dagger , Per JonassonDagger Dagger §§, Martin LinhultDagger Dagger , Per-Åke NygrenDagger Dagger , Mathias UhlénDagger Dagger , Lars Björck, Torbjörn DrakenbergDagger , Sture ForsénDagger , and Mats Wikström||

From the Dagger  Department of Biophysical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, the  Department of Cell and Molecular Biology, Section for Pathogenesis, BMC, B14, Lund University, Tornavägen 10, SE-221 84 Lund, || Biovitrum AB, Nordenflychtsvägen 62:5, SE-112 76 Stockholm, and the Dagger Dagger  Department of Biotechnology, Royal Institute of Technology (KTH), Stockholms Centrum för Fysik Astronomi Bioteknik, S-106 91 Stockholm, Sweden

We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics.

* This work was supported by Swedish Research Council Projects 7480 (to L. B.) and 31X-13088-03C (to T. D.). The 600 MHz spectrometer (Lund University) used in this study was purchased by a grant from the Knut and Alice Wallenberg Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The 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 the structure factors (code 1GJS (ensemble) and 1GJT (structure closest to the average)) 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: Dept. of Biophysical Chemistry, Lund University, P. O. Box 124, Lund SE-221 00, Sweden. Fax: 46-46-222-4543; E-mail: maria.johansson@bpc.lu.se.

** Present address: Stockholm Bioinformatics Center, Dept. of Biochemistry and Biophysics, Stockholm University, Stockholm S-106 91, Sweden.

§§ Present address: AstraZeneca Biotech Laboratory, EST-Biology, Södertälje S-151 85, Sweden.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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