Structure, specificity, and mode of interaction for bacterial albumin-binding modules.
Författare
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.
Avdelning/ar
Publiceringsår
2002
Språk
Engelska
Sidor
8114-8120
Publikation/Tidskrift/Serie
Journal of Biological Chemistry
Volym
277
Issue
10
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Biochemistry and Molecular Biology
Ämne
- Physical Chemistry
Nyckelord
- 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/Övrigt
- ISSN: 1083-351X