9BNH
X-ray Crystal Structure of Cu-TZ4H tryptophan Zipper Metallo-Peptide
Summary for 9BNH
| Entry DOI | 10.2210/pdb9bnh/pdb |
| Descriptor | Cu-TZ4H tryptophan Zipper Metallo-Peptide, AMMONIA, ACETIC ACID, ... (7 entities in total) |
| Functional Keywords | copper, beta-sheet, hairpin, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 4183.38 |
| Authors | Dang, V.T.,Nguyen, A. (deposition date: 2024-05-02, release date: 2024-09-04, Last modification date: 2024-11-06) |
| Primary citation | Thuc Dang, V.,Engineer, A.,McElheny, D.,Drena, A.,Telser, J.,Tomczak, K.,Nguyen, A.I. Crystallography Reveals Metal-Triggered Restructuring of beta-Hairpins. Chemistry, 30:e202402101-e202402101, 2024 Cited by PubMed Abstract: Metal binding to β-sheets occurs in many metalloproteins and is also implicated in the pathology of Alzheimer's disease. De novo designed metallo-β-sheets have been pursued as models and mimics of these proteins. However, no crystal structures of canonical β-sheet metallopeptides have yet been obtained, in stark contrast to many examples for ɑ-helical metallopeptides, leading to a poor understanding for their chemistry. To address this, we have engineered tryptophan zippers, stable 12-residue β-sheet peptides, to bind Cu(II) ions and obtained crystal structures through single crystal X-ray diffraction (SC-XRD). We find that metal binding triggers several unexpected supramolecular assemblies that demonstrate the range of higher-order structures available to metallo-β-sheets. Overall, these findings underscore the importance of crystallography in elucidating the rich structural landscape of metallo-β-sheet peptides. PubMed: 39152095DOI: 10.1002/chem.202402101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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