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Structure, specificity, and mode of interaction for bacterial albumin-binding modules.

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Summary, in English

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.

Publishing year

2002

Language

English

Pages

8114-8120

Publication/Series

Journal of Biological Chemistry

Volume

277

Issue

10

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Physical Chemistry

Keywords

  • Binding Competitive
  • Circular Dichroism
  • Dose-Response Relationship Drug
  • Drug Resistance
  • Evolution Molecular
  • Inhibitory Concentration 50
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models Molecular
  • Molecular Sequence Data
  • Peptostreptococcus : metabolism
  • Protein Binding
  • Sequence Homology Amino Acid
  • Rabbits
  • Binding Sites
  • Amino Acid Sequence
  • Animal
  • Serum Albumin : chemistry : metabolism
  • Substrate Specificity
  • Support Non-U.S. Gov't
  • Temperature

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X