2fha: Difference between revisions
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[[Image:2fha.gif|left|200px]]<br /><applet load="2fha" size=" | [[Image:2fha.gif|left|200px]]<br /><applet load="2fha" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fha, resolution 1.9Å" /> | caption="2fha, resolution 1.9Å" /> | ||
'''HUMAN H CHAIN FERRITIN'''<br /> | '''HUMAN H CHAIN FERRITIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2FHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=FOX:These Residues Form The Catalytic Ferroxidase Center Whi ...'>FOX</scene>. Full crystallographic information is available from [http:// | 2FHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=FOX:These+Residues+Form+The+Catalytic+Ferroxidase+Center+Whi+...'>FOX</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: iron storage]] | [[Category: iron storage]] | ||
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Revision as of 11:37, 3 February 2008
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HUMAN H CHAIN FERRITIN
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[134770]
About this StructureAbout this Structure
2FHA is a Single protein structure of sequence from Homo sapiens with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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