3EEX
The crystal structure of OspA mutant
Summary for 3EEX
| Entry DOI | 10.2210/pdb3eex/pdb |
| Descriptor | Outer Surface Protein A, HEXAETHYLENE GLYCOL (2 entities in total) |
| Functional Keywords | beta-sheet, membrane protein |
| Biological source | Borrelia burgdorferi |
| Total number of polymer chains | 2 |
| Total formula weight | 69704.13 |
| Authors | Makabe, K.,Biancalana, M.,Koide, S. (deposition date: 2008-09-06, release date: 2009-09-08, Last modification date: 2023-08-30) |
| Primary citation | Biancalana, M.,Makabe, K.,Koide, S. Minimalist design of water-soluble cross-{beta} architecture. Proc.Natl.Acad.Sci.USA, 107:3469-3474, 2010 Cited by PubMed Abstract: Demonstrated successes of protein design and engineering suggest significant potential to produce diverse protein architectures and assemblies beyond those found in nature. Here, we describe a new class of synthetic protein architecture through the successful design and atomic structures of water-soluble cross-beta proteins. The cross-beta motif is formed from the lamination of successive beta-sheet layers, and it is abundantly observed in the core of insoluble amyloid fibrils associated with protein-misfolding diseases. Despite its prominence, cross-beta has been designed only in the context of insoluble aggregates of peptides or proteins. Cross-beta's recalcitrance to protein engineering and conspicuous absence among the known atomic structures of natural proteins thus makes it a challenging target for design in a water-soluble form. Through comparative analysis of the cross-beta structures of fibril-forming peptides, we identified rows of hydrophobic residues ("ladders") running across beta-strands of each beta-sheet layer as a minimal component of the cross-beta motif. Grafting a single ladder of hydrophobic residues designed from the Alzheimer's amyloid-beta peptide onto a large beta-sheet protein formed a dimeric protein with a cross-beta architecture that remained water-soluble, as revealed by solution analysis and x-ray crystal structures. These results demonstrate that the cross-beta motif is a stable architecture in water-soluble polypeptides and can be readily designed. Our results provide a new route for accessing the cross-beta structure and expanding the scope of protein design. PubMed: 20133689DOI: 10.1073/pnas.0912654107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.49 Å) |
Structure validation
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