1oqu
From Proteopedia
(New page: 200px<br /><applet load="1oqu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqu, resolution 2.0Å" /> '''A protein coordinated...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size=" | + | [[Image:1oqu.gif|left|200px]]<br /><applet load="1oqu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oqu, resolution 2.0Å" /> | 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 /> | '''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of an oxo-centered tri-nuclear iron complex formed | + | 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== | ==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:// | + | 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== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: tri-iron]] | [[Category: tri-iron]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:33 2008'' |
Revision as of 12:20, 21 February 2008
|
A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes
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.
About this Structure
1OQU is a Single protein structure of sequence from Corynebacterium ammoniagenes with , and as ligands. Full crystallographic information is available from OCA.
Reference
A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization., Hogbom M, Nordlund P, FEBS Lett. 2004 Jun 4;567(2-3):179-82. PMID:15178319
Page seeded by OCA on Thu Feb 21 14:20:33 2008
Categories: Corynebacterium ammoniagenes | Single protein | Hogbom, M. | Nordlund, P. | ACT | FE | OXY | Ferritin | Glutamate | Mineralization | Tri-iron
