2fha
From Proteopedia
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| - | [[Image:2fha.gif|left|200px]] | + | [[Image:2fha.gif|left|200px]] |
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| - | '''HUMAN H CHAIN FERRITIN''' | + | {{Structure |
| + | |PDB= 2fha |SIZE=350|CAPTION= <scene name='initialview01'>2fha</scene>, resolution 1.9Å | ||
| + | |SITE= <scene name='pdbsite=FOX:These+Residues+Form+The+Catalytic+Ferroxidase+Center+Whi+...'>FOX</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN H CHAIN FERRITIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FHA is a [ | + | 2FHA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHA OCA]. |
==Reference== | ==Reference== | ||
| - | Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:[http:// | + | Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9159481 9159481] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[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 16:52:28 2008'' |
Revision as of 14:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN H CHAIN FERRITIN
Contents |
Overview
Mammalian ferritins are 24-mers assembled from two types of polypeptide chain which provide the molecule with different functions. H(eavy) chains catalyse the first step in iron storage, the oxidation of iron(II). L(ight) chains promote the nucleation of the mineral ferrihydrite enabling storage of iron(III) inside the protein shell. We report here the comparison of the three-dimensional structures of recombinant human H chain (HuHF) and horse L chain (HoLF) ferritin homopolymers, which have been refined at 1.9 A resolution. There is 53% sequence identity between these molecules, and the two structures are very similar, the H and L subunit alpha-carbons superposing to within 0.5 A rms deviation with 41 water molecules in common. Nevertheless, there are significant important differences which can be related to differences in function. In particular, the centres of the four-helix bundles contain distinctive groups of hydrophilic residues which have been associated with ferroxidase activity in H chains and enhanced stability in L chains. L chains contain a group of glutamates associated with mineralisation within the iron storage cavity of the protein.
Disease
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[134770]
About this Structure
2FHA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:9159481
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