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1BG7

LOCALIZED UNFOLDING AT THE JUNCTION OF THREE FERRITIN SUBUNITS. A MECHANISM FOR IRON RELEASE?

Summary for 1BG7
Entry DOI10.2210/pdb1bg7/pdb
DescriptorFERRITIN, CALCIUM ION (3 entities in total)
Functional Keywordsferritin, iron storage
Biological sourceRana catesbeiana (bullfrog)
Total number of polymer chains1
Total formula weight20586.18
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 citationTakagi, 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: 9668036
DOI: 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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