6IWJ
A designed domain swapped dimer
Summary for 6IWJ
| Entry DOI | 10.2210/pdb6iwj/pdb |
| Descriptor | Archeal Protein MK0293 (1 entity in total) |
| Functional Keywords | complex, domain-swapping, archea, protein design, unknown function |
| Biological source | Methanopyrus kandleri AV19 |
| Total number of polymer chains | 2 |
| Total formula weight | 22647.53 |
| Authors | Nandwani, N.,Negi, H.,Das, R. (deposition date: 2018-12-05, release date: 2019-02-13, Last modification date: 2024-05-15) |
| Primary citation | Nandwani, N.,Surana, P.,Negi, H.,Mascarenhas, N.M.,Udgaonkar, J.B.,Das, R.,Gosavi, S. A five-residue motif for the design of domain swapping in proteins. Nat Commun, 10:452-452, 2019 Cited by PubMed Abstract: Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two β-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse β-hairpin proteins. PubMed: 30692525DOI: 10.1038/s41467-019-08295-x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
