1gjs
From Proteopedia
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SOLUTION STRUCTURE OF THE ALBUMIN BINDING DOMAIN OF STREPTOCOCCAL PROTEIN G
Overview
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.
About this Structure
1GJS is a Single protein structure of sequence from Streptococcus sp. group g. Full crystallographic information is available from OCA.
Reference
Structure, specificity, and mode of interaction for bacterial albumin-binding modules., Johansson MU, Frick IM, Nilsson H, Kraulis PJ, Hober S, Jonasson P, Linhult M, Nygren PA, Uhlen M, Bjorck L, Drakenberg T, Forsen S, Wikstrom M, J Biol Chem. 2002 Mar 8;277(10):8114-20. Epub 2001 Dec 18. PMID:11751858
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