9G3U
Crystal Structure of the artificial protein METP in complex with cadmium ion at different temperatures. Room temperature data collection
Summary for 9G3U
| Entry DOI | 10.2210/pdb9g3u/pdb |
| Descriptor | METP artificial protein, CADMIUM ION (3 entities in total) |
| Functional Keywords | de novo design, room temperature, cadmium-sulphur cluster, denovo protein, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 3067.66 |
| Authors | Di Costanzo, L.,La Gatta, S.,Chino, M. (deposition date: 2024-07-12, release date: 2024-12-04, Last modification date: 2025-01-22) |
| Primary citation | Di Costanzo, L.F.,Sgueglia, G.,Orlando, C.,Polentarutti, M.,Leone, L.,La Gatta, S.,De Fenza, M.,De Gioia, L.,Lombardi, A.,Arrigoni, F.,Chino, M. Structural insights into temperature-dependent dynamics of METPsc1, a miniaturized electron-transfer protein. J.Inorg.Biochem., 264:112810-112810, 2025 Cited by PubMed Abstract: The design of protein-metal complexes is rapidly advancing, with applications spanning catalysis, sensing, and bioremediation. We report a comprehensive investigation of METPsc1, a Miniaturized Electron Transfer Protein, in complex with cadmium. This study elucidates the impact of metal coordination on protein folding and structural dynamics across temperatures from 100 K to 300 K. Our findings reveal that METPsc1, composed of two similar halves stabilized by intramolecular hydrogen bonds, exhibits a unique "clothespin-like" recoil mechanism. This allows it to adapt to metal ions of varying radii, mirroring the flexibility observed in natural rubredoxins. High-resolution crystallography and molecular dynamics simulations unveil concerted backbone motions and subtle temperature-dependent shifts in side-chain conformations, particularly for residues involved in crystal packing. Notably, CdS bond lengths increase with temperature, correlating with anisotropic motions of the sulfur atoms involved in second-shell hydrogen bonding. This suggests a dynamic role of protein matrix upon redox cycling. These insights into METPsc1 highlight its potential for catalysis and contribute to the designing of artificial metalloproteins with functional plasticity. PubMed: 39689412DOI: 10.1016/j.jinorgbio.2024.112810 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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