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PDBsum entry 1qqw
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Oxidoreductase
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PDB id
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1qqw
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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 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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Abstract
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Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized
in three different forms: orthorhombic, hexagonal and tetragonal. The structure
of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space
group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A,
was determined and refined with 2.75 A resolution data. Non-crystallographic
symmetry restraints were employed and the resulting R value and R(free) were
0.206 and 0.272, respectively. The overall structure and arrangement of HEC
molecules in the orthorhombic unit cell were very similar to those of bovine
liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a
water was bound to the active-site residue His75. Conserved lattice interactions
suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
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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
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2000,
56,
241-245)
copyright 2000.
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