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PDBsum entry 1f4j
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Oxidoreductase
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PDB id
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1f4j
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of tetragonal crystals of human erythrocyte catalase.
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Authors
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M.K.Safo,
F.N.Musayev,
S.H.Wu,
D.J.Abraham,
T.P.Ko.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1-7.
[DOI no: ]
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PubMed id
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Abstract
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The structure of catalase from human erythrocytes (HEC) was determined in
tetragonal crystals of space group I4(1) by molecular-replacement methods, using
the orthorhombic crystal structure as a search model. It was then refined in a
unit cell of dimensions a = b = 203.6 and c = 144.6 A, yielding R and R(free) of
0.196 and 0.244, respectively, for all data at 2.4 A resolution. A major
difference of the HEC structure in the tetragonal crystal compared with the
orthorhombic structure was the omission of a 20-residue N-terminal segment
corresponding to the first exon of the human catalase gene. The overall
structures were otherwise identical in both crystal forms. The NADPH-binding
sites were empty in all four subunits and bound water molecules were observed at
the active sites. The structure of the C-terminal segment, which corresponds to
the last exon, remained undetermined. The tetragonal crystals showed a
pseudo-4(1)22 symmetry in molecular packing. Two similar types of lattice
contact interfaces between the HEC tetramers were observed; they were related by
the pseudo-dyad axes.
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Figure 1.
Figure 1 Comparison of catalase structures from different
organisms. The subunit models of (a) HEC and BLC, shown in
orange and red, respectively, (b) HPII and PVC, in green and
cyan, respectively, (c) SCCA and PMC, in magenta and blue,
respectively, and (d) all six catalases were superimposed by O
and the protein backbones were drawn using GRASP. The heme group
is shown in red. NADPH is not shown. The position of Lys23 in
HEC is indicated by an arrow in (a).
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Figure 2.
Figure 2 Difference Fourier (2F[o] - F[c]) maps of the four heme
groups in the tetragonal HEC crystal. Maps were calculated using
the final model and contoured at 1.0  level,
colored cyan. The heme groups of subunits A, B, C and D are
shown in (a), (b), (c) and (d), respectively, with bonds in
pink. Also shown are the residues His75, Asn148, Arg354 and
Tyr358, as well as one or two active-site water molecules,
colored green. The figures were produced using BobScript and
Raster3D.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1-7)
copyright 2001.
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Secondary reference #1
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Title
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Structure of human erythrocyte catalase.
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Authors
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T.P.Ko,
M.K.Safo,
F.N.Musayev,
M.L.Di salvo,
C.Wang,
S.H.Wu,
D.J.Abraham.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2000,
56,
241-245.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2 Superposition of the HEC (colored blue) and BLC
(colored purple) models. The C^  atoms
of the variable residues are shown in green. Heme groups are
shown in red. The NADPH molecules which were observed in BLC but
not in HEC are shown in yellow. The figure was drawn using GRASP.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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