8W7U
Mutant of ferritin from Ureaplasma diversum (Udif-E164A-E168A) without soaking
Summary for 8W7U
Entry DOI | 10.2210/pdb8w7u/pdb |
Related | 8W6M |
Descriptor | Ferritin, FE (III) ION, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | ferritin, iron, fe-o cluster, 4-fold channel cavity, metal binding protein |
Biological source | Ureaplasma diversum |
Total number of polymer chains | 1 |
Total formula weight | 21386.61 |
Authors | Wang, W.M.,Xi, H.F.,Gong, W.J.,Ma, D.Y.,Wang, H.F. (deposition date: 2023-08-31, release date: 2024-06-12) |
Primary citation | Wang, W.,Xi, H.,Fu, D.,Ma, D.,Gong, W.,Zhao, Y.,Li, X.,Wu, L.,Guo, Y.,Zhao, G.,Wang, H. Growth Process of Fe-O Nanoclusters with Different Sizes Biosynthesized by Protein Nanocages. J.Am.Chem.Soc., 146:11657-11668, 2024 Cited by PubMed Abstract: All protein-directed syntheses of metal nanoclusters (NCs) and nanoparticles (NPs) have attracted considerable attention because protein scaffolds provide a unique metal coordination environment and can adjust the shape and morphology of NCs and NPs. However, the detailed formation mechanisms of NCs or NPs directed by protein templates remain unclear. In this study, by taking advantage of the ferritin nanocage as a biotemplate to monitor the growth of Fe-O NCs as a function of time, we synthesized a series of iron NCs with different sizes and shapes and subsequently solved their corresponding three-dimensional atomic-scale structures by X-ray protein crystallography and cryo-electron microscopy. The time-dependent structure analyses revealed the growth process of these Fe-O NCs with the 4-fold channel of ferritin as nucleation sites. To our knowledge, the newly biosynthesized FeOGlu represents the largest Fe-O NCs with a definite atomic structure. This study contributes to our understanding of the formation mechanism of iron NCs and provides an effective method for metal NC synthesis. PubMed: 38641862DOI: 10.1021/jacs.3c13830 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.502 Å) |
Structure validation
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