1s3q
From Proteopedia
(New page: 200px<br /><applet load="1s3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s3q, resolution 2.10Å" /> '''Crystal structures o...) |
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| - | [[Image:1s3q.gif|left|200px]]<br /><applet load="1s3q" size=" | + | [[Image:1s3q.gif|left|200px]]<br /><applet load="1s3q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s3q, resolution 2.10Å" /> | caption="1s3q, resolution 2.10Å" /> | ||
'''Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus'''<br /> | '''Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ferritins are known as important iron storage/detoxification proteins and | + | Ferritins are known as important iron storage/detoxification proteins and are widely found in living organisms. This report details the 2.1 A resolution native and 2.7 A resolution iron bound structures of the ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus, and represents the first structure of a ferritin from an archaeon, or a hyperthermophilic organism. The A. fulgidus ferritin (AfFtn) monomer has a high degree of structural similarity with archetypal ferritins from E. coli and humans, but the AfFtn quaternary structure is novel; 24 subunits assemble into a shell having tetrahedral (2-3) rather than the canonical octahedral (4-3-2) symmetry of archetypal ferritins. The difference in assembly opens four large (approximately 45 A) pores in the AfFtn shell. Two nonconservative amino acid substitutions may be critical for stabilizing the tetrahedral form. |
==About this Structure== | ==About this Structure== | ||
| - | 1S3Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1S3Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: iron storage]] | [[Category: iron storage]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:36 2008'' |
Revision as of 12:57, 21 February 2008
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Crystal structures of a novel open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus
Overview
Ferritins are known as important iron storage/detoxification proteins and are widely found in living organisms. This report details the 2.1 A resolution native and 2.7 A resolution iron bound structures of the ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus, and represents the first structure of a ferritin from an archaeon, or a hyperthermophilic organism. The A. fulgidus ferritin (AfFtn) monomer has a high degree of structural similarity with archetypal ferritins from E. coli and humans, but the AfFtn quaternary structure is novel; 24 subunits assemble into a shell having tetrahedral (2-3) rather than the canonical octahedral (4-3-2) symmetry of archetypal ferritins. The difference in assembly opens four large (approximately 45 A) pores in the AfFtn shell. Two nonconservative amino acid substitutions may be critical for stabilizing the tetrahedral form.
About this Structure
1S3Q is a Single protein structure of sequence from Archaeoglobus fulgidus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic archaeon Archaeoglobus fulgidus., Johnson E, Cascio D, Sawaya MR, Gingery M, Schroder I, Structure. 2005 Apr;13(4):637-48. PMID:15837202
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