From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1rcg.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rcg.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1rcg| PDB=1rcg | SCENE= }} | | {{STRUCTURE_1rcg| PDB=1rcg | SCENE= }} |
| | | | |
| - | '''BULLFROG RED CELL L FERRITIN SULFATE/MN/PH 6.3'''
| + | ===BULLFROG RED CELL L FERRITIN SULFATE/MN/PH 6.3=== |
| | | | |
| | | | |
| - | ==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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7760335}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7760335 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_7760335}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 26: |
Line 30: |
| | [[Category: Trikha, J.]] | | [[Category: Trikha, J.]] |
| | [[Category: Iron storage]] | | [[Category: Iron storage]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:19:54 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:21:56 2008'' |
Revision as of 17:22, 27 July 2008
Template:STRUCTURE 1rcg
BULLFROG RED CELL L FERRITIN SULFATE/MN/PH 6.3
Template:ABSTRACT PUBMED 7760335
About this Structure
1RCG 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 Sun Jul 27 20:21:56 2008
