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

Publiceringsår: 2002
Språk: Engelska
Sidor: 8114-8120
Publikation/Tidskrift/Serie: Journal of Biological Chemistry
Volym: 277
Nummer: 10
Dokumenttyp: Artikel i tidskrift
Förlag: ASBMB


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.


  • Physical Chemistry
  • 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


  • ISSN: 1083-351X

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