6LJY
A Crystal Structure of OspA mutant
Summary for 6LJY
| Entry DOI | 10.2210/pdb6ljy/pdb |
| Descriptor | OspA163 (2 entities in total) |
| Functional Keywords | outer surface protein a, ospa, lipid binding protein |
| Biological source | Borreliella burgdorferi |
| Total number of polymer chains | 1 |
| Total formula weight | 25416.32 |
| Authors | Kiya, M.,Makabe, K. (deposition date: 2019-12-17, release date: 2020-12-23, Last modification date: 2024-02-21) |
| Primary citation | Kiya, M.,Shiga, S.,Ding, P.,Koide, S.,Makabe, K. beta-Strand-mediated Domain-swapping in the Absence of Hydrophobic Core Repacking. J.Mol.Biol., 436:168405-168405, 2024 Cited by PubMed Abstract: Domain swapping is a process wherein a portion of a protein is exchanged with its counterpart in another copy of the molecule, resulting in the formation of homo-oligomers with concomitant repacking of a hydrophobic core. Here, we report domain swapping triggered upon modifying a β-hairpin sequence within a single-layer β-sheet (SLB) of a model protein, OspA that did not involve the formation of a reorganized hydrophobic core. The replacement of two β-hairpin sequences with a Gly-Gly and shorteing of a β-hairpin resulted in a protein that formed two distinct crystal structures under similar conditions: one was monomeric, similar to the parental molecule, whereas the other was a domain-swapped dimer, mediated by an intermolecular β-sheet in the SLB portion. Based on the dimer interface structure, we replaced the Gly-Gly sequence with three-residue sequences that enable the formation of a consecutive intermolecular β-sheet, including the Cys-Thr-Cys sequence that formed a stable disulfide-linked dimer. These results provide new insights into protein folding, evolution, and the designability of protein structure. PubMed: 38104859DOI: 10.1016/j.jmb.2023.168405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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