1ZSZ
Crystal structure of a computationally designed SspB heterodimer
Summary for 1ZSZ
| Entry DOI | 10.2210/pdb1zsz/pdb |
| Descriptor | Stringent starvation protein B homolog, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | protein design, aaa, adaptor, specificity, de novo protein |
| Biological source | Haemophilus influenzae More |
| Total number of polymer chains | 3 |
| Total formula weight | 39931.56 |
| Authors | Bolon, D.N.,Grant, R.A.,Baker, T.A.,Sauer, R.T. (deposition date: 2005-05-25, release date: 2005-08-23, Last modification date: 2023-08-23) |
| Primary citation | Bolon, D.N.,Grant, R.A.,Baker, T.A.,Sauer, R.T. Specificity versus stability in computational protein design. Proc.Natl.Acad.Sci.Usa, 102:12724-12729, 2005 Cited by PubMed Abstract: Protein-protein interactions can be designed computationally by using positive strategies that maximize the stability of the desired structure and/or by negative strategies that seek to destabilize competing states. Here, we compare the efficacy of these methods in reengineering a protein homodimer into a heterodimer. The stability-design protein (positive design only) was experimentally more stable than the specificity-design heterodimer (positive and negative design). By contrast, only the specificity-design protein assembled as a homogenous heterodimer in solution, whereas the stability-design protein formed a mixture of homodimer and heterodimer species. The experimental stabilities of the engineered proteins correlated roughly with their calculated stabilities, and the crystal structure of the specificity-design heterodimer showed most of the predicted side-chain packing interactions and a main-chain conformation indistinguishable from the wild-type structure. These results indicate that the design simulations capture important features of both stability and structure and demonstrate that negative design can be critical for attaining specificity when competing states are close in structure space. PubMed: 16129838DOI: 10.1073/pnas.0506124102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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