3CKF
The crystal structure of OspA deletion mutant
Summary for 3CKF
| Entry DOI | 10.2210/pdb3ckf/pdb |
| Related | 3CKA 3CKG |
| Descriptor | Outer surface protein A (2 entities in total) |
| Functional Keywords | beta-sheet, membrane protein |
| Biological source | Borrelia burgdorferi (Lyme disease spirochete) More |
| Total number of polymer chains | 1 |
| Total formula weight | 23852.65 |
| Authors | Makabe, K.,Koide, S. (deposition date: 2008-03-14, release date: 2009-01-27, Last modification date: 2023-08-30) |
| Primary citation | Makabe, K.,Koide, S. The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion J.Am.Chem.Soc., 130:14370-14371, 2008 Cited by PubMed Abstract: Recent studies suggest the dominant role of main-chain H-bond formation in specifying beta-sheet topology. Its essentially sequence-independent nature implies a large degree of freedom in designing beta-sheet-based nanomaterials. Here we show rational design of beta-sheet face inversions by incremental deletions of beta-strands from the single-layer beta-sheet of Borrelia outer surface protein A. We show that a beta-sheet structure can be maintained when a large number of native contacts are removed and that one can design large-scale conformational transitions of a beta-sheet such as face inversion by exploiting the promiscuity of strand-strand interactions. High-resolution X-ray crystal structures confirmed the success of the design and supported the importance of main-chain H-bonds in determining beta-sheet topology. This work suggests a simple but effective strategy for designing and controlling nanomaterials based on beta-rich peptide self-assemblies. PubMed: 18842042DOI: 10.1021/ja805011h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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