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Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin

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Author

Summary, in English

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 Angstrom 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.

Publishing year

2004

Language

English

Pages

42924-42928

Publication/Series

Journal of Biological Chemistry

Volume

279

Issue

41

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Infectious Medicine

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X