1oqu: Difference between revisions

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[[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1oqu, resolution 2.0Å" />

'''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes'''<br />

==Overview==

The crystal structure of an oxo-centered tri-nuclear iron complex formed, on a protein surface is presented. The cluster forms when crystals of the, class Ib ribonucleotide reductase R2 protein from Corynebacterium, ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is, coordinated by protein-derived carboxylate ligands arranged in a motif, similar to the one found on the inner surface of ferritins and may mimic, an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.

The crystal structure of an oxo-centered tri-nuclear iron complex formed on a protein surface is presented. The cluster forms when crystals of the class Ib ribonucleotide reductase R2 protein from Corynebacterium ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is coordinated by protein-derived carboxylate ligands arranged in a motif similar to the one found on the inner surface of ferritins and may mimic an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.

==About this Structure==

1OQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes] with FE, ACT and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA].

1OQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA].

==Reference==

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[[Category: tri-iron]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 01~~:17:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:33 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1oqu, resolution 2.0&Aring;" />
 '''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes'''<br />
 ==Overview==
-The crystal structure of an oxo-centered tri-nuclear iron complex formed, on a protein surface is presented. The cluster forms when crystals of the, class Ib ribonucleotide reductase R2 protein from Corynebacterium, ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is, coordinated by protein-derived carboxylate ligands arranged in a motif, similar to the one found on the inner surface of ferritins and may mimic, an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.
+The crystal structure of an oxo-centered tri-nuclear iron complex formed on a protein surface is presented. The cluster forms when crystals of the class Ib ribonucleotide reductase R2 protein from Corynebacterium ammoniagenes are subjected to iron soaking. The tri-iron-oxo complex is coordinated by protein-derived carboxylate ligands arranged in a motif similar to the one found on the inner surface of ferritins and may mimic an early stage in the mineralization of iron in ferritins. In addition, the structure adds to the very limited data on protein-mineral interfaces.
 ==About this Structure==
-OQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes] with FE, ACT and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA].
+OQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: tri-iron]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:17:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:33 2008''