9QHC
Crystal structure of 8-repeat CTPR protein with eliminated coordination sites
Summary for 9QHC
| Entry DOI | 10.2210/pdb9qhc/pdb |
| Descriptor | Engineered tetratricopeptide repeat protein, CALCIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | crystal engineering, protein engineering, de novo protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 68698.77 |
| Authors | |
| Primary citation | Liutkus, M.,Rojas, A.L.,Cortajarena, A.L. Rational Crystal Contact Engineering for Programmable Self-Assembled Protein Architectures. Angew.Chem.Int.Ed.Engl., :e202516635-e202516635, 2025 Cited by PubMed Abstract: Ordered protein-based assemblies are increasingly desirable for materials science, but the design of new materials remains challenging and requires considerable effort. Crystal lattice contact modulation enables rapid rational design of an assortment of structurally diverse constructs with crystalline order. Targeted disruption of crystal contacts and directional growth pre-biasing allows for restricting crystal lattice growth in selected directions, resulting in lower-dimension assemblies with parent crystal structural features. Two-dimensional crystals, one-dimensional fibres, flexible ribbons, and single-walled nanotubes based on tetratricopeptide repeat proteins were constructed from reengineered 3D crystal lattices. The large library of available crystal structures provides an abundance of engineering targets, promising to make crystal contact engineering a rapid and attractive approach for the design of ordered supramolecular protein assemblies. PubMed: 41077847DOI: 10.1002/anie.202516635 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.88 Å) |
Structure validation
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