1oqu

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{{STRUCTURE_1oqu| PDB=1oqu | SCENE= }}
{{STRUCTURE_1oqu| PDB=1oqu | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15178319 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15178319}}
==About this Structure==
==About this Structure==
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[[Category: Mineralization]]
[[Category: Mineralization]]
[[Category: Tri-iron]]
[[Category: Tri-iron]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:10:23 2008''
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Revision as of 20:18, 28 July 2008

Template:STRUCTURE 1oqu

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

Template:ABSTRACT PUBMED 15178319

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 Mon Jul 28 23:18:24 2008

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