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PDBsum entry 2htn
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Metal binding protein, oxidoreductase
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PDB id
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2htn
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References listed in PDB file
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Key reference
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Title
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Fortuitous structure determination of 'As-Isolated' Escherichia coli bacterioferritin in a novel crystal form.
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Authors
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A.Van eerde,
S.Wolterink-Van loo,
J.Van der oost,
B.W.Dijkstra.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2006,
62,
1061-1066.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3 The ferroxidase centre. (a) Stereo figures of  [A]-weighted
F[o] - F[c] density in the ferroxidase site contoured at 5 ,
(b) superposition of the ferroxidase centre of the P2[1]3
structure (grey/orange) and the Mn-bound structure
(yellow/purple; PDB code 1bcf ; Frolow et al., 1994[Frolow, F.,
Kalb, A. J. & Yariv, J. (1994). Nature Struct. Biol. 1,
453-460.]) of E. coli bacterioferritin and (c) superposition of
the FE2 site environment in the P2[1]3 E. coli bacterioferritin
structure (grey) with the corresponding region in the structure
of reduced A. vinelandii bacterioferritin (pale green; PDB code
1fkz ; Swartz et al., 2006[Swartz, L., Kuchinskas, M., Li, H.,
Poulos, T. L. & Lanzilotta, W. N. (2006). Biochemistry, 45,
4421-4428.]). The location of the inner cavity (IC) is
indicated. This view is rotated  90°
with respect to the previous views.
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Figure 4.
Figure 4 X-ray fluorescence scans around the K edges of Mn, Fe,
Cu and Zn, as indicated. Plots are corrected for beam intensity
and fluorescence is on an arbitrary scale.
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The above figures are
reprinted
from an Open Access publication published by the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2006,
62,
1061-1066)
copyright 2006.
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