6KK9
A Crystal structure of OspA mutant
Summary for 6KK9
| Entry DOI | 10.2210/pdb6kk9/pdb |
| Descriptor | Outer Surface Protein A (2 entities in total) |
| Functional Keywords | outer surface protein a, lipid binding protein |
| Biological source | Borreliella burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 4 |
| Total formula weight | 87472.95 |
| Authors | Shiga, S.,Makabe, K. (deposition date: 2019-07-24, release date: 2020-07-29, Last modification date: 2023-11-22) |
| Primary citation | Shiga, S.,Makabe, K. Structural analysis of the beta-sheet edge of peptide self-assembly using a model protein. Proteins, 89:845-852, 2021 Cited by PubMed Abstract: Peptides and proteins self-assemble into β-sheet-rich fibrils, amyloid, which extends its structure by incorporating peptide/protein molecules from solution. At the elongation edge, the peptide/protein molecule binds to the edge of the amyloid β-sheet. Such processes are transient and elusive when observing molecular details by experimental methods. We used a model protein system, peptide self-assembly mimic (PSAM), which mimics an amyloid-like structure within a globular protein by capping both edges of single-layer β sheet (SLB) with certain domains. We constructed a PSAM variant that lacks the capping domain on the C-terminal side to observe the structure of the β-sheet edge of the peptide self-assembly. This variant, which we termed PSAM-edge, proved to be soluble with a monomeric form. Urea-induced unfolding experiments revealed that PSAM-edge displayed two-state cooperative unfolding, indicating the N-terminal capping domain and extended SLB folded as one unit. The crystal structure showed that SLB was almost completely structured except for a few terminal residues. A molecular dynamics simulation results revealed that the SLB structure was retained while the C-terminal four residues fluctuated, which was consistent with the crystal structure. Our findings indicate that SLB is stable even when one side of the β-sheet edge is exposed to a solvent. This stability may prevent the dissociation of the attached peptide from the peptide self-assembly. Because of the scarcity of SLB proteins with exposed β-sheet edges in nature, successful construction of the PSAM-edge expands our understanding of protein folding and design. PubMed: 33576533DOI: 10.1002/prot.26063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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