Structure, specificity, and mode of interaction for bacterial albumin-binding modules
2002 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 277, no 10, 8114-8120 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
2002. Vol. 277, no 10, 8114-8120 p.
streptococcal protein-g, human-serum-albumin, igg-binding, immunoglobulin-g, b-domain, group-c, x-ray, nmr, evolution, identification
IdentifiersURN: urn:nbn:se:kth:diva-21366DOI: 10.1074/jbc.M109943200ISI: 000174268000063OAI: oai:DiVA.org:kth-21366DiVA: diva2:340064
QC 201005252010-08-102010-08-10Bibliographically approved