 |
|
|
 |
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
160 a.a.
Key reference
Acta Crystallogr D Biol Crystallogr 58:29-38 (2002) PubMed id: 11752777
The 2.6 A resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'. D.Cobessi, L.S.Huang, M.Ban, N.G.Pon, F.Daldal, E.A.Berry. ABSTRACT
Bacterioferritin from Rhodobacter capsulatus was crystallized and its structure was solved at 2.6 A resolution. This first structure of a bacterioferritin from a photosynthetic organism is a spherical particle of 24 subunits displaying 432 point-group symmetry like ferritin and bacterioferritin from Escherichia coli. Crystallized in the I422 space group, its structural analysis reveals for the first time the non-symmetric heme molecule located on a twofold crystallographic symmetry axis. Other hemes of the protomer are situated on twofold noncrystallographic axes. Apparently, both types of sites bind heme in two orientations, leading to an average structure consisting of a symmetric 50:50 mixture, thus satisfying the crystallographic and noncrystallographic symmetry of the crystal. Five water molecules are situated close to the heme, which is bound in a hydrophobic pocket and axially coordinated by two crystallographic or noncrystallographically related methionine residues. Its ferroxidase center, in which Fe(II) is oxidized to Fe(III), is empty or fractionally occupied by a metal ion. Two positions are observed for the coordinating Glu18 side chain instead of one in the E. coli enzyme in which the site is occupied. This result suggests that the orientation of the Glu18 side chain could be constrained by this interaction.
Literature references that cite this PDB file's key reference
PubMed id Reference
19439409 S.G.Wong, S.A.Tom-Yew, A.Lewin, N.E.Le Brun, G.R.Moore, M.E.Murphy, and A.G.Mauk (2009).
Structural and Mechanistic Studies of a Stabilized Subunit Dimer Variant of Escherichia coli Bacterioferritin Identify Residues Required for Core Formation.J Biol Chem, 284, 18873-18881.
PDB code: 3e2c
18445621 R.Janowski, T.Auerbach-Nevo, and M.S.Weiss (2008).
Bacterioferritin from Mycobacterium smegmatis contains zinc in its di-nuclear site.Protein Sci, 17, 1138-1150.
PDB code: 3bkn 17077480 A.van Eerde, S.Wolterink-van Loo, J.van der Oost, and B.W.Dijkstra (2006).
Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1061-1066.
PDB code: 2htn
12727864 M.A.Carrondo (2003).
Ferritins, iron uptake and storage from the bacterioferritin viewpoint.EMBO J, 22, 1959-1968.
12876316 M.A.Kilic, S.Spiro, and G.R.Moore (2003).
Stability of a 24-meric homopolymer: comparative studies of assembly-defective mutants of Rhodobacter capsulatus bacterioferritin and the native protein.Protein Sci, 12, 1663-1674.
12704186 M.Moche, J.Shanklin, A.Ghoshal, and Y.Lindqvist (2003).
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates.J Biol Chem, 278, 25072-25080.
PDB codes: 1oq4 1oq7 1oq9 1oqb
12627224 S.Macedo, C.V.Romão, E.Mitchell, P.M.Matias, M.Y.Liu, A.V.Xavier, J.LeGall, M.Teixeira, P.Lindley, and M.A.Carrondo (2003).
The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans.Nat Struct Biol, 10, 285-290.
PDB codes: 1nf4 1nf6 1nfv The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
