1oqu
From Proteopedia
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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
