1sof

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(New page: 200px<br /><applet load="1sof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sof, resolution 2.60&Aring;" /> '''Crystal structure of...)
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[[Image:1sof.gif|left|200px]]<br /><applet load="1sof" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sof.gif|left|200px]]<br /><applet load="1sof" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sof, resolution 2.60&Aring;" />
caption="1sof, resolution 2.60&Aring;" />
'''Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution'''<br />
'''Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution'''<br />
==Overview==
==Overview==
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The crystal structure of the bacterioferritin from Azotobacter vinelandii, has been determined at 2.6 A resolution. Both the low occupancy of one, iron ion in the dinuclear iron center and the deviation of its adjacent, residue His130 from the center suggest migration of the iron ion from the, dinuclear iron site to the inner nucleation site. The concerted movement, of His130 and Glu47 may admit a dynamic gating mechanism for shift of the, oxidized iron ion. Ba2+ binding to the fourfold channel implicates that, the channel bears Fe2+ conductivity and selectivity to provide a route for, iron access to the inner cavity during core formation.
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The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba2+ binding to the fourfold channel implicates that the channel bears Fe2+ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.
==About this Structure==
==About this Structure==
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1SOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with FE2, MG, BA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SOF OCA].
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1SOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=BA:'>BA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOF OCA].
==Reference==
==Reference==
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bi, R.C.]]
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[[Category: Bi, R C.]]
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[[Category: Huang, J.F.]]
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[[Category: Huang, J F.]]
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[[Category: Liu, H.L.]]
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[[Category: Liu, H L.]]
[[Category: BA]]
[[Category: BA]]
[[Category: FE2]]
[[Category: FE2]]
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[[Category: four-helix bundle]]
[[Category: four-helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:31:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:37 2008''

Revision as of 13:03, 21 February 2008

Image:1sof.gif

1sof, resolution 2.60Å

Drag the structure with the mouse to rotate

Crystal structure of the azotobacter vinelandii bacterioferritin at 2.6 A resolution

Overview

The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba2+ binding to the fourfold channel implicates that the channel bears Fe2+ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.

About this Structure

1SOF is a Single protein structure of sequence from Azotobacter vinelandii with , , and as ligands. Full crystallographic information is available from OCA.

Reference

2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii., Liu HL, Zhou HN, Xing WM, Zhao JF, Li SX, Huang JF, Bi RC, FEBS Lett. 2004 Aug 27;573(1-3):93-8. PMID:15327981

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