2htn
From Proteopedia
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, resolution 2.50Å | |||||||
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Ligands: | and | ||||||
Activity: | Ferroxidase, with EC number 1.16.3.1 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
E. coli bacterioferritin in its as-isolated form
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. 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 Mar 20 17:21:28 2008