1BG7
LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?
Summary for 1BG7
Entry DOI | 10.2210/pdb1bg7/pdb |
Descriptor | FERRITIN, CALCIUM ION (3 entities in total) |
Functional Keywords | ferritin, iron storage |
Biological source | Rana catesbeiana (bullfrog) |
Total number of polymer chains | 1 |
Total formula weight | 20586.18 |
Authors | Takagi, H.,Shi, D.,Ha, Y.,Allewell, N.M.,Theil, E.C. (deposition date: 1998-06-05, release date: 1999-01-13, Last modification date: 2024-05-22) |
Primary citation | Takagi, H.,Shi, D.,Ha, Y.,Allewell, N.M.,Theil, E.C. Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J.Biol.Chem., 273:18685-18688, 1998 Cited by PubMed Abstract: How and where iron exits from ferritin for cellular use is unknown. Twenty-four protein subunits create a cavity in ferritin where iron is concentrated >10(11)-fold as a mineral. Proline substitution for conserved leucine 134 (L134P) allowed normal assembly but increased iron exit rates. X-ray crystallography of H-L134P ferritin revealed localized unfolding at the 3-fold axis, also iron entry sites, consistent with shared use sites for iron exit and entry. The junction of three ferritin subunits appears to be a dynamic aperture with a "shutter" that cytoplasmic factors might open or close to regulate iron release in vivo. PubMed: 9668036DOI: 10.1074/jbc.273.30.18685 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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