1Q10
Ensemble of 40 Structures of the Dimeric Mutant of the B1 Domain of Streptococcal Protein G
Summary for 1Q10
| Entry DOI | 10.2210/pdb1q10/pdb |
| Related | 1GB1 1MPE |
| Descriptor | Immunoglobulin G binding protein G (1 entity in total) |
| Functional Keywords | gb1, core mutants, domain-swapping, oligomerization, protein binding |
| Biological source | Streptococcus sp. 'group G' |
| Cellular location | Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654 |
| Total number of polymer chains | 2 |
| Total formula weight | 12453.67 |
| Authors | Byeon, I.J.,Louis, J.M.,Gronenborn, A.M. (deposition date: 2003-07-18, release date: 2003-10-14, Last modification date: 2024-05-22) |
| Primary citation | Byeon, I.J.,Louis, J.M.,Gronenborn, A.M. A Protein Contortionist: Core Mutations of GB1 that Induce Dimerization and Domain Swapping J.Mol.Biol., 333:141-152, 2003 Cited by PubMed Abstract: Immunoglobulin-binding domain B1 of streptococcal protein G (GB1), a small (56 residues), stable, single-domain protein, is one of the most extensively used model systems in the area of protein folding and design. Recently, NMR and X-ray structures of a quintuple GB1 core mutant (L5V/A26F/F30V/Y33F/A34F) that showed an unexpected, intertwined tetrameric architecture were determined. Here, we report the NMR structure of another mutant, derived from the tetramer by reverting the single amino acid position F26 back to the wild-type sequence A26. The structure reveals a domain-swapped dimer that involves exchange of the second beta-hairpin. The resulting overall structure comprises an eight-stranded beta-sheet whose concave side is covered by two alpha helices. The dimer dissociates into a partially folded, monomeric species with a dissociation constant of 93(+/-10)microM. PubMed: 14516749DOI: 10.1016/S0022-2836(03)00928-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
