1tk6: Difference between revisions
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[[Image:1tk6.gif|left|200px]] | [[Image:1tk6.gif|left|200px]] | ||
'''Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states''' | {{Structure | ||
|PDB= 1tk6 |SIZE=350|CAPTION= <scene name='initialview01'>1tk6</scene>, resolution 2.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TK6 is a [ | 1TK6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TK6 OCA]. | ||
==Reference== | ==Reference== | ||
Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states., Zeth K, Offermann S, Essen LO, Oesterhelt D, Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13780-5. Epub 2004 Sep 13. PMID:[http:// | Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states., Zeth K, Offermann S, Essen LO, Oesterhelt D, Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13780-5. Epub 2004 Sep 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15365182 15365182] | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: low-iron]] | [[Category: low-iron]] | ||
''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 14:19:27 2008'' | ||
Revision as of 15:19, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Iron-oxo clusters biomineralizing on protein surfaces. Structural analysis of H.salinarum DpsA in its low and high iron states
OverviewOverview
The crystal structure of the Dps-like (Dps, DNA-protecting protein during starvation) ferritin protein DpsA from the halophile Halobacterium salinarum was determined with low endogenous iron content at 1.6-A resolution. The mechanism of iron uptake and storage was analyzed in this noncanonical ferritin by three high-resolution structures at successively increasing iron contents. In the high-iron state of the DpsA protein, up to 110 iron atoms were localized in the dodecameric protein complex. For ultimate iron storage, the archaeal ferritin shell comprises iron-binding sites for iron translocation, oxidation, and nucleation. Initial iron-protein interactions occur through acidic residues exposed along the outer surface in proximity to the iron entry pore. This narrow pore permits translocation of ions toward the ferroxidase centers via two discrete steps. Iron oxidation proceeds by transient formation of tri-iron ferroxidase centers. Iron storage by biomineralization inside the ferritin shell occurs at two iron nucleation centers. Here, a single iron atom provides a structural seed for iron-oxide cluster formation. The clusters with up to five iron atoms adopt a geometry that is different from natural biominerals like magnetite but resembles iron clusters so far known only from bioinorganic model compounds.
About this StructureAbout this Structure
1TK6 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
ReferenceReference
Iron-oxo clusters biomineralizing on protein surfaces: structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states., Zeth K, Offermann S, Essen LO, Oesterhelt D, Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13780-5. Epub 2004 Sep 13. PMID:15365182
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