1GJS
Solution structure of the Albumin binding domain of Streptococcal Protein G
Summary for 1GJS
| Entry DOI | 10.2210/pdb1gjs/pdb |
| Related | 1FCC 1FCL 1FD6 1GB4 1GJT 1IBX 1P7E 1P7F 2IGG |
| Descriptor | IMMUNOGLOBULIN G BINDING PROTEIN G (1 entity in total) |
| Functional Keywords | immunoglobulin-binding protein, bacterial surface protein, albumin binding, protein g |
| Biological source | STREPTOCOCCUS SP. (GROUP G STREPTOCOCCI) |
| Cellular location | Secreted, cell wall ; Peptidoglycan-anchor : P19909 |
| Total number of polymer chains | 1 |
| Total formula weight | 7111.09 |
| Authors | Johansson, M.U.,Frick, I.M.,Nilsson, H.,Kraulis, P.J.,Hober, S.,Jonasson, P.,Nygren, A.P.,Uhlen, M.,Bjorck, L.,Drakenberg, T.,Forsen, S.,Wikstrom, M. (deposition date: 2001-08-02, release date: 2001-08-09, Last modification date: 2024-05-15) |
| Primary citation | Johansson, M.,Frick, I.,Nilsson, H.,Kraulis, P.,Hober, S.,Jonasson, P.,Linhult, M.,Nygren, P.,Uhlen, M.,Bjorck, L.,Drakenberg, T.,Forsen, S.,Wikstrom, M. Structure, Specificity, and Mode of Interaction for Bacterial Albumin-Binding Modules J.Biol.Chem., 277:8114-, 2002 Cited by PubMed Abstract: 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. PubMed: 11751858DOI: 10.1074/JBC.M109943200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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