1fha: Difference between revisions
New page: left|200px<br /> <applet load="1fha" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fha, resolution 2.4Å" /> '''SOLVING THE STRUCTUR... |
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[[Image:1fha.gif|left|200px]]<br /> | [[Image:1fha.gif|left|200px]]<br /><applet load="1fha" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1fha, resolution 2.4Å" /> | caption="1fha, resolution 2.4Å" /> | ||
'''SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS'''<br /> | '''SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS'''<br /> | ||
==Overview== | ==Overview== | ||
Ferritin is important in iron homeostasis. Its twenty-four chains of two | Ferritin is important in iron homeostasis. Its twenty-four chains of two types, H and L, assemble as a hollow shell providing an iron-storage cavity. Ferritin molecules in cells containing high levels of iron tend to be rich in L chains, and may have a long-term storage function, whereas H-rich ferritins are more active in iron metabolism. The molecular basis for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown owing to the difficulties in obtaining crystals ordered enough for X-ray crystallographic analysis. Here we report the three-dimensional structure of a human ferritin H-chain homopolymer. By genetically engineering a change in the sequence of the intermolecular contact region, we obtained crystals isomorphous with the homologous rat L ferritin and of high enough quality for X-ray diffraction analysis. The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and we suggest that ferroxidase activity associated with this site accounts for its rapid uptake of iron. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1FHA 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 FE and CA as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1FHA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb35_1.html Ferritin and Transferrin]]. Full crystallographic information is available from [http:// | 1FHA 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=FE:'>FE</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1FHA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb35_1.html Ferritin and Transferrin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Artymiuk, P | [[Category: Artymiuk, P J.]] | ||
[[Category: Harrison, P | [[Category: Harrison, P M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: FE]] | [[Category: FE]] | ||
[[Category: iron storage]] | [[Category: iron storage]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:38:38 2008'' | ||
Revision as of 13:38, 21 February 2008
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SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS
OverviewOverview
Ferritin is important in iron homeostasis. Its twenty-four chains of two types, H and L, assemble as a hollow shell providing an iron-storage cavity. Ferritin molecules in cells containing high levels of iron tend to be rich in L chains, and may have a long-term storage function, whereas H-rich ferritins are more active in iron metabolism. The molecular basis for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown owing to the difficulties in obtaining crystals ordered enough for X-ray crystallographic analysis. Here we report the three-dimensional structure of a human ferritin H-chain homopolymer. By genetically engineering a change in the sequence of the intermolecular contact region, we obtained crystals isomorphous with the homologous rat L ferritin and of high enough quality for X-ray diffraction analysis. The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and we suggest that ferroxidase activity associated with this site accounts for its rapid uptake of iron.
DiseaseDisease
Known diseases associated with this structure: Iron overload, autosomal dominant OMIM:[134770]
About this StructureAbout this Structure
1FHA is a Single protein structure of sequence from Homo sapiens with and as ligands. The following page contains interesting information on the relation of 1FHA with [Ferritin and Transferrin]. Full crystallographic information is available from OCA.
ReferenceReference
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts., Lawson DM, Artymiuk PJ, Yewdall SJ, Smith JM, Livingstone JC, Treffry A, Luzzago A, Levi S, Arosio P, Cesareni G, et al., Nature. 1991 Feb 7;349(6309):541-4. PMID:1992356
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