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1rci
From Proteopedia
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| - | [[Image:1rci.gif|left|200px]] | + | [[Image:1rci.gif|left|200px]] |
| - | + | ||
| - | '''BULLFROG RED CELL L FERRITIN TARTRATE/MG/PH 5.5''' | + | {{Structure |
| + | |PDB= 1rci |SIZE=350|CAPTION= <scene name='initialview01'>1rci</scene>, resolution 2.0Å | ||
| + | |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== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RCI is a [ | + | 1RCI 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=1RCI OCA]. |
==Reference== | ==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:// | + | 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: Rana catesbeiana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: iron storage]] | [[Category: iron storage]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:43 2008'' |
Revision as of 11:49, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Gene: | CDNA (Rana catesbeiana) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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-->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.
About this Structure
1RCI is a Single protein structure of sequence from Rana catesbeiana. Full crystallographic information is available from 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:7760335
Page seeded by OCA on Thu Mar 20 13:49:43 2008
