3AJQ
Crystal structure of human H ferritin E140Q mutant
Summary for 3AJQ
| Entry DOI | 10.2210/pdb3ajq/pdb |
| Related | 3AJO 3AJP |
| Descriptor | Ferritin heavy chain, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | 4-helix-bundle, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 21390.83 |
| Authors | Masuda, T.,Mikami, B. (deposition date: 2010-06-11, release date: 2010-08-25, Last modification date: 2024-04-03) |
| Primary citation | Masuda, T.,Goto, F.,Yoshihara, T.,Mikami, B. The universal mechanism for iron translocation to the ferroxidase site in ferritin, which is mediated by the well conserved transit site Biochem.Biophys.Res.Commun., 400:94-99, 2010 Cited by PubMed Abstract: Ferritins are ubiquitous iron storage proteins. Recently, we identified a novel metal-binding site, transit site, in the crystal structure of phytoferritin. To elucidate the function of the transit site in ferritin from other species, we prepared transit-site-deficient mutants of human H ferritin, E140A and E140Q, and their iron oxidation kinetics was analyzed. The initial velocities of iron oxidization were reduced in the variants, especially in E140Q. The crystal structure of E140Q showed that the side chain of the mutated Gln140 was fixed by a hydrogen bond, whereas that of native Glu140 was flexible. These results suggest that the conserved transit site also has a function to assist with the metal ion sequestration to the ferroxidase site in ferritins from vertebrates. PubMed: 20705053DOI: 10.1016/j.bbrc.2010.08.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
Download full validation report
