1RCC

BULLFROG RED CELL L FERRITIN TARTRATE/MG/PH 5.5

Summary for 1RCC

• Entry DOI: 10.2210/pdb1rcc/pdb
• Descriptor: L FERRITIN, TRIMETHYL GLYCINE (3 entities in total)
• Functional Keywords: iron storage
• Biological source: Rana catesbeiana (bullfrog)
• Total number of polymer chains: 1
• Total formula weight: 19853.34

Authors

Trikha, J.,Theil, E.C.,Allewell, N.M. (deposition date: 1995-08-04, release date: 1995-11-14, Last modification date: 2023-11-15)

Primary citation

Trikha, J.,Theil, E.C.,Allewell, N.M.
High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function.
J.Mol.Biol., 248:949-967, 1995

PubMed Abstract: Ferritin is a highly conserved multisubunit protein in animals, plants and microbes which assembles with cubic symmetry and transports hydrated iron ions and protons to and from a mineralized core in the protein interior. We report here the high resolution structures of recombinant amphibian red-cell L ferritin and two mutants solved under two sets of conditions. In one mutant, Glu56, 57, 58 and 60 were replaced with Ala, producing a lag phase in the kinetics of iron uptake. In the second mutant, His25 was replaced with Tyr with, at most, subtle effects on function. A molecule of betaine, used in the purification, is bound in all structures at the 2-fold axis near the recently identified heme binding site of bacterioferritin and horse spleen L ferritin. Comparisons of the five amphibian structures identify two regions of the molecule in which conformational flexibility may be related to function. The positions and interactions of a set of 10 to 18 side-chains, most of which are on the inner surface of the protein, are sensitive both to solution conditions and to the Glu-->Ala mutation. A subset of these side-chains and a chain of ordered solvent molecules extends from the vicinity of Glu56 to 58 and Glu60 to the 3-fold channel in the wild type protein and may be involved in the transport of either iron or protons. The "spine of hydration" is disrupted in the Glu-->Ala mutant. In contrast, H25Y mutation shifts the positions of backbone atoms between the site of the mutation and the 4-fold axis and side-chain positions throughout the structure; the largest changes in the position of backbone atoms are in the DE loop and E helix, approximately 10 A from the mutation site. In combination, these results indicate that solvation, structural plasticity and cooperative structural changes may play a role in ferritin function. Analogies with the structure and function of ion channel proteins such as annexins are noted.

PubMed: 7760335
DOI: 10.1006/jmbi.1995.0274

Experimental method

X-RAY DIFFRACTION (2.4 Å)