5OFS
X-ray structure of a zinc binding GB1 mutant
Summary for 5OFS
| Entry DOI | 10.2210/pdb5ofs/pdb |
| Related | 5O94 |
| Descriptor | Immunoglobulin G-binding protein G, ZINC ION, ACETATE ION, ... (9 entities in total) |
| Functional Keywords | immunoglobulin bindi, metal binding protein |
| Biological source | Streptococcus sp. group G |
| Total number of polymer chains | 4 |
| Total formula weight | 26893.61 |
| Authors | Rothlisberger, U.,Bozkurt, E.,Hovius, R.,Perez, M.A.S.,Browning, N.J. (deposition date: 2017-07-11, release date: 2018-04-04, Last modification date: 2024-01-17) |
| Primary citation | Bozkurt, E.,Perez, M.A.S.,Hovius, R.,Browning, N.J.,Rothlisberger, U. Genetic Algorithm Based Design and Experimental Characterization of a Highly Thermostable Metalloprotein. J. Am. Chem. Soc., 140:4517-4521, 2018 Cited by PubMed Abstract: The development of thermostable and solvent-tolerant metalloproteins is a long-sought goal for many applications in synthetic biology and biotechnology. In this work, we were able to engineer a highly thermostable and organic solvent-stable metallo variant of the B1 domain of protein G (GB1) with a tetrahedral zinc binding site reminiscent of the one of thermolysin. Promising candidates were designed computationally by applying a protocol based on classical and first-principles molecular dynamics simulations in combination with genetic algorithm optimization. The most promising of the computationally predicted mutants was expressed and structurally characterized and yielded a highly thermostable protein. The experimental results thus confirm the predictive power of the applied computational protein engineering approach for the de novo design of highly stable metalloproteins. PubMed: 29336153DOI: 10.1021/jacs.7b10660 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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