8H8M
Crystal structure of apo-E53F/E57F/E60F/E64F-rHLFr
Summary for 8H8M
| Entry DOI | 10.2210/pdb8h8m/pdb |
| Descriptor | Ferritin light chain, 1,2-ETHANEDIOL, CADMIUM ION, ... (6 entities in total) |
| Functional Keywords | ferritin, metal binding protein |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 21071.53 |
| Authors | Hishikawa, Y.,Noya, H.,Maity, B.,Abe, S.,Ueno, T. (deposition date: 2022-10-23, release date: 2023-10-04) |
| Primary citation | Hishikawa, Y.,Noya, H.,Nagatoishi, S.,Yoshidome, T.,Maity, B.,Tsumoto, K.,Abe, S.,Ueno, T. Elucidating Conformational Dynamics and Thermostability of Designed Aromatic Clusters by Using Protein Cages. Chemistry, 29:e202300488-e202300488, 2023 Cited by PubMed Abstract: Multiple aromatic residues assemble to form higher ordered structures known as "aromatic clusters" in proteins and play essential roles in biological systems. However, the stabilization mechanism and dynamic behavior of aromatic clusters remain unclear. This study describes designed aromatic interactions confined within a protein cage to reveal how aromatic clusters affect protein stability. The crystal structures and calorimetric measurements indicate that the formation of inter-subunit phenylalanine clusters enhance the interhelix interactions and increase the melting temperature. Theoretical calculations suggest that this is caused by the transformation of the T-shaped geometry into π-π stacking at high temperatures, and the hydration entropic gain. Thus, the isolated nanoenvironment in a protein cage allows reconstruction and detailed analysis of multiple clustering residues for elucidating the mechanisms of various biomolecular interactions in nature which can be applied to design of bionanomaterials. PubMed: 37070368DOI: 10.1002/chem.202300488 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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