1OQU

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

Summary for 1OQU

Entry DOI	10.2210/pdb1oqu/pdb
Related	1kgn 1kgo 1kgp
Descriptor	ribonucleotide reductase subunit R2F, FE (III) ION, OXYGEN MOLECULE, ... (5 entities in total)
Functional Keywords	mineralization, ferritin, tri-iron, glutamate, metal binding protein
Biological source	Corynebacterium ammoniagenes
Total number of polymer chains	4
Total formula weight	153108.03
Authors	Hogbom, M.,Nordlund, P. (deposition date: 2003-03-11, release date: 2004-04-20, Last modification date: 2024-03-13)
Primary citation	Hogbom, M.,Nordlund, P. A protein carboxylate coordinated oxo-centered tri-nuclear iron complex with possible implications for ferritin mineralization Febs Lett., 567:179-182, 2004 Cited by PubMed Abstract: 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. PubMed: 15178319 DOI: 10.1016/j.febslet.2004.04.068 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation