1oqu
From Proteopedia
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| - | [[Image:1oqu.gif|left|200px]] | + | [[Image:1oqu.gif|left|200px]] |
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| - | '''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes''' | + | {{Structure |
| + | |PDB= 1oqu |SIZE=350|CAPTION= <scene name='initialview01'>1oqu</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=OXY:OXYGEN MOLECULE'>OXY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''A protein coordinated tri-nuclear Fe complex formed during soaking of crystals of the ribonucleotide reductase R2F protein from Corynebacterium Ammoniagenes''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OQU is a [ | + | 1OQU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_ammoniagenes Corynebacterium ammoniagenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15178319 15178319] |
[[Category: Corynebacterium ammoniagenes]] | [[Category: Corynebacterium ammoniagenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tri-iron]] | [[Category: tri-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 13:14:24 2008'' |
Revision as of 11:14, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 13:14:24 2008
Categories: Corynebacterium ammoniagenes | Single protein | Hogbom, M. | Nordlund, P. | ACT | FE | OXY | Ferritin | Glutamate | Mineralization | Tri-iron
