View source for 1rcd

[[Image:1rcd.gif|left|200px]]

 {{Structure
|PDB= 1rcd |SIZE=350|CAPTION= <scene name='initialview01'>1rcd</scene>, resolution 2.0&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=BET:TRIMETHYL GLYCINE'>BET</scene>
|ACTIVITY= 
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8400 Rana catesbeiana])
}}

'''BULLFROG RED CELL L FERRITIN TARTRATE/MG/PH 5.5'''


==Overview==
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--&gt;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--&gt;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.

==About this Structure==
1RCD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rana_catesbeiana Rana catesbeiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCD OCA]. 

==Reference==
High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function., Trikha J, Theil EC, Allewell NM, J Mol Biol. 1995 May 19;248(5):949-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7760335 7760335]
[[Category: Rana catesbeiana]]
[[Category: Single protein]]
[[Category: Allewell, N M.]]
[[Category: Theil, E C.]]
[[Category: Trikha, J.]]
[[Category: BET]]
[[Category: iron storage]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:39 2008''