3AUM
Crystal structure of OspA mutant
Summary for 3AUM
| Entry DOI | 10.2210/pdb3aum/pdb |
| Descriptor | Outer surface protein A (2 entities in total) |
| Functional Keywords | beta-mender, membrane protein |
| Biological source | Borrelia burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 1 |
| Total formula weight | 26939.00 |
| Authors | Makabe, K. (deposition date: 2011-02-10, release date: 2012-02-15, Last modification date: 2023-11-01) |
| Primary citation | Biancalana, M.,Makabe, K.,Yan, S.,Koide, S. Aromatic cluster mutations produce focal modulations of beta-sheet structure. Protein Sci., 24:841-849, 2015 Cited by PubMed Abstract: Site-directed mutagenesis is a powerful tool for altering the structure and function of proteins in a focused manner. Here, we examined how a model β-sheet protein could be tuned by mutation of numerous surface-exposed residues to aromatic amino acids. We designed these aromatic side chain "clusters" at highly solvent-exposed positions in the flat, single-layer β-sheet of Borrelia outer surface protein A (OspA). This unusual β-sheet scaffold allows us to interrogate the effects of these mutations in the context of well-defined structure but in the absence of the strong scaffolding effects of globular protein architecture. We anticipated that the introduction of a cluster of aromatic amino acid residues on the β-sheet surface would result in large conformational changes and/or stabilization and thereby provide new means of controlling the properties of β-sheets. Surprisingly, X-ray crystal structures revealed that the introduction of aromatic clusters produced only subtle conformational changes in the OspA β-sheet. Additionally, despite burying a large degree of hydrophobic surface area, the aromatic cluster mutants were slightly less stable than the wild-type scaffold. These results thereby demonstrate that the introduction of aromatic cluster mutations can serve as a means for subtly modulating β-sheet conformation in protein design. PubMed: 25645104DOI: 10.1002/pro.2657 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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