6NJ6
Thermostable variant of human carbonic anhydrase with tetrazine 2.0 at site 186 reacted with sTCO in crystallo
Summary for 6NJ6
| Entry DOI | 10.2210/pdb6nj6/pdb |
| Descriptor | Carbonic anhydrase 2, METHANOL, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | genetic code expansion, thermostability, protein engineering, lyase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 61619.50 |
| Authors | Kean, K.M.,Karplus, P.A. (deposition date: 2019-01-02, release date: 2019-10-02, Last modification date: 2023-10-11) |
| Primary citation | Bednar, R.M.,Golbek, T.W.,Kean, K.M.,Brown, W.J.,Jana, S.,Baio, J.E.,Karplus, P.A.,Mehl, R.A. Immobilization of Proteins with Controlled Load and Orientation. ACS Appl Mater Interfaces, 11:36391-36398, 2019 Cited by PubMed Abstract: Biomaterials based on immobilized proteins are key elements of many biomedical and industrial technologies. However, applications are limited by an inability to precisely construct materials of high homogeneity and defined content. We present here a general "protein-limited immobilization" strategy by combining the rapid, bioorthogonal, and biocompatible properties of a tetrazine-strained -cyclooctene reaction with genetic code expansion to site-specifically place the tetrazine into a protein. For the first time, we use this strategy to immobilize defined amounts of oriented proteins onto beads and flat surfaces in under 5 min at submicromolar concentrations without compromising activity. This approach opens the door to generating and studying diverse protein-based biomaterials that are much more precisely defined and characterized, providing a greater ability to engineer properties across a wide range of applications. PubMed: 31525993DOI: 10.1021/acsami.9b12746 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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