2HKD
The crystal structure of engineered OSPA
Summary for 2HKD
| Entry DOI | 10.2210/pdb2hkd/pdb |
| Descriptor | Outer Surface Protein A, TETRAETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | beta sheet, engineered protein, de novo protein |
| Biological source | Borreliella burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 1 |
| Total formula weight | 34576.43 |
| Authors | Makabe, K.,Terechko, V.,Koide, S. (deposition date: 2006-07-03, release date: 2006-11-21, Last modification date: 2023-08-30) |
| Primary citation | Makabe, K.,McElheny, D.,Tereshko, V.,Hilyard, A.,Gawlak, G.,Yan, S.,Koide, A.,Koide, S. Atomic structures of peptide self-assembly mimics. Proc.Natl.Acad.Sci.Usa, 103:17753-17758, 2006 Cited by PubMed Abstract: Although the beta-rich self-assemblies are a major structural class for polypeptides and the focus of intense research, little is known about their atomic structures and dynamics due to their insoluble and noncrystalline nature. We developed a protein engineering strategy that captures a self-assembly segment in a water-soluble molecule. A predefined number of self-assembling peptide units are linked, and the beta-sheet ends are capped to prevent aggregation, which yields a mono-dispersed soluble protein. We tested this strategy by using Borrelia outer surface protein (OspA) whose single-layer beta-sheet located between two globular domains consists of two beta-hairpin units and thus can be considered as a prototype of self-assembly. We constructed self-assembly mimics of different sizes and determined their atomic structures using x-ray crystallography and NMR spectroscopy. Highly regular beta-sheet geometries were maintained in these structures, and peptide units had a nearly identical conformation, supporting the concept that a peptide in the regular beta-geometry is primed for self-assembly. However, we found small but significant differences in the relative orientation between adjacent peptide units in terms of beta-sheet twist and bend, suggesting their inherent flexibility. Modeling shows how this conformational diversity, when propagated over a large number of peptide units, can lead to a substantial degree of nanoscale polymorphism of self-assemblies. PubMed: 17093048DOI: 10.1073/pnas.0606690103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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