6ICS
Loop deletion mutant (deleting four residues)
Summary for 6ICS
| Entry DOI | 10.2210/pdb6ics/pdb |
| Descriptor | Outer surface protein A (2 entities in total) |
| Functional Keywords | outer surface protein a, ospa, lipid binding protein, de novo protein |
| Biological source | Borrelia burgdorferi |
| Total number of polymer chains | 1 |
| Total formula weight | 26079.16 |
| Authors | Shiga, S.,Makabe, K. (deposition date: 2018-09-06, release date: 2019-07-03, Last modification date: 2023-11-22) |
| Primary citation | Shiga, S.,Yamanaka, M.,Fujiwara, W.,Hirota, S.,Goda, S.,Makabe, K. Domain-Swapping Design by Polyproline Rod Insertion. Chembiochem, 20:2454-2457, 2019 Cited by PubMed Abstract: During domain swapping, proteins mutually interconvert structural elements to form a di-/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, a simple design strategy is shown for domain-swapping formation by loop deletion and insertion of a polyproline rod. Crystal structures revealed the formation of the domain-swapped dimers and polyproline portion formed a polyproline II (PPII) structure. Small-angle X-ray scattering demonstrated that an extended orientation of domain-swapped dimer was retained in solution. It is found that a multiple of three of inserting proline residue is favored for domain swapping because of the helical nature of PPII. The rigid nature of the polyproline rod enables precise control of the interdomain distance and orientation. PubMed: 31094059DOI: 10.1002/cbic.201900179 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
