This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2htn
From Proteopedia
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| 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
