2htn | pdb_00002htn
E. coli bacterioferritin in its as-isolated form
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Overview
Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is different from that of previous structures and is a mix of zinc and native iron ions. The ferroxidase-centre configuration displays a similar flexibility as previously noted for other bacterioferritins.
About this Structure
2HTN is a Single protein structure of sequence from Escherichia coli with FE and HEM as ligands. Active as Ferroxidase, with EC number 1.16.3.1 Full crystallographic information is available from OCA.
Reference
Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form., van Eerde A, Wolterink-van Loo S, van der Oost J, Dijkstra BW, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1061-6. Epub 2006 Oct 25. PMID:17077480
Page seeded by OCA on Thu Feb 21 17:45:35 2008
