2HTN

E. coli bacterioferritin in its as-isolated form

Summary for 2HTN

• Entry DOI: 10.2210/pdb2htn/pdb
• Descriptor: Bacterioferritin, FE (III) ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: four-helix bundle, ferroxidase centre, haem, protein shell, iron binding site, metal binding protein, oxidoreductase
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 151503.60

Authors

van Eerde, A.,Wolterink-Van Loo, S.,Van Der Oost, J.,Dijkstra, B.W. (deposition date: 2006-07-26, release date: 2006-11-21, Last modification date: 2023-08-30)

Primary citation

van Eerde, A.,Wolterink-van Loo, S.,van der Oost, J.,Dijkstra, B.W.
Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.
Acta Crystallogr.,Sect.F, 62:1061-1066, 2006

PubMed Abstract: 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.

PubMed: 17077480
DOI: 10.1107/S1744309106039583

Experimental method

X-RAY DIFFRACTION (2.5 Å)