7E3E
Crystal structure of Trypanosoma brucei cathepsin B R91C/T223C mutant
Summary for 7E3E
Entry DOI | 10.2210/pdb7e3e/pdb |
Descriptor | Cysteine peptidase C (CPC), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
Functional Keywords | in cell crystal, hydrolase |
Biological source | Trypanosoma brucei brucei (strain 927/4 GUTat10.1) |
Total number of polymer chains | 1 |
Total formula weight | 38218.62 |
Authors | Abe, S.,Pham, T.T.,Negishi, H.,Yamashita, K.,Hirata, K.,Ueno, T. (deposition date: 2021-02-08, release date: 2021-12-15, Last modification date: 2024-11-13) |
Primary citation | Abe, S.,Pham, T.T.,Negishi, H.,Yamashita, K.,Hirata, K.,Ueno, T. Design of an In-Cell Protein Crystal for the Environmentally Responsive Construction of a Supramolecular Filament. Angew.Chem.Int.Ed.Engl., 60:12341-12345, 2021 Cited by PubMed Abstract: Protein assemblies can be designed for development of nano-bio materials. This has been achieved by modulating protein-protein interactions. However, fabrication of highly ordered protein assemblies remains challenging. Protein crystals, which have highly ordered arrangements of protein molecules, provide useful source matrices for synthesizing artificial protein assemblies. Here, we describe construction of a supramolecular filament structure by engineering covalent and non-covalent interactions in a protein crystal. Performing in-cell crystallization of Trypanosoma brucei cysteine protease cathepsin B (TbCatB), we achieved a precise arrangement of protein molecules while suppressing random aggregation due to disulfide bonds. We succeeded in synthesizing bundled filament from the crystals by autoxidation of cysteinyl thiols after the isolation of the crystals from living cells. PubMed: 33759310DOI: 10.1002/anie.202102039 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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