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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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PDB id:
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Oxidoreductase
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Title:
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Crystal structure of human erythrocyte catalase
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Structure:
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Catalase. Chain: a, b, c, d. Ec: 1.11.1.6
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: erythrocyte
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Biol. unit:
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Tetramer (from
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Resolution:
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2.75Å
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R-factor:
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0.206
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R-free:
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0.272
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Authors:
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T.P.Ko,M.K.Safo,F.N.Musayev,C.Wang,S.H.Wu,D.J.Abraham
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Key ref:
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T.P.Ko
et al.
(2000).
Structure of human erythrocyte catalase.
Acta Crystallogr D Biol Crystallogr,
56,
241-245.
PubMed id:
DOI:
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Date:
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09-Jun-99
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Release date:
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14-Jun-99
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PROCHECK
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Headers
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References
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P04040
(CATA_HUMAN) -
Catalase from Homo sapiens
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Seq:
Struc:
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527 a.a.
499 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.1.11.1.6
- catalase.
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Reaction:
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2 H2O2 = O2 + 2 H2O
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2
×
H2O2
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=
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O2
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+
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2
×
H2O
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Cofactor:
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Heme; Mn(2+)
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Heme
Bound ligand (Het Group name =
HEM)
matches with 95.45% similarity
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Mn(2+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr D Biol Crystallogr
56:241-245
(2000)
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PubMed id:
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Structure of human erythrocyte catalase.
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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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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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Selected figure(s)
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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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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Rusu,
and
S.Birmanns
(2010).
Evolutionary tabu search strategies for the simultaneous registration of multiple atomic structures in cryo-EM reconstructions.
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J Struct Biol,
170,
164-171.
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S.Pakhomova,
B.Gao,
W.E.Boeglin,
A.R.Brash,
and
M.E.Newcomer
(2009).
The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis.
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Protein Sci,
18,
2559-2568.
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PDB codes:
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B.Gao,
W.E.Boeglin,
and
A.R.Brash
(2008).
Role of the conserved distal heme asparagine of coral allene oxide synthase (Asn137) and human catalase (Asn148): mutations affect the rate but not the essential chemistry of the enzymatic transformations.
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Arch Biochem Biophys,
477,
285-290.
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Z.He,
S.Yu,
G.Mei,
M.Zheng,
M.Wang,
Y.Dai,
B.Tang,
and
N.Li
(2008).
Maternally transmitted milk containing recombinant human catalase provides protection against oxidation for mouse offspring during lactation.
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Free Radic Biol Med,
45,
1135-1142.
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J.I.Koepke,
K.A.Nakrieko,
C.S.Wood,
K.K.Boucher,
L.J.Terlecky,
P.A.Walton,
and
S.R.Terlecky
(2007).
Restoration of peroxisomal catalase import in a model of human cellular aging.
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Traffic,
8,
1590-1600.
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M.Niepmann
(2007).
Discontinuous native protein gel electrophoresis: pros and cons.
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Expert Rev Proteomics,
4,
355-361.
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D.E.Heck,
A.M.Vetrano,
T.M.Mariano,
and
J.D.Laskin
(2003).
UVB light stimulates production of reactive oxygen species: unexpected role for catalase.
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J Biol Chem,
278,
22432-22436.
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W.Melik-Adamyan,
J.Bravo,
X.Carpena,
J.Switala,
M.J.Maté,
I.Fita,
and
P.C.Loewen
(2001).
Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli.
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Proteins,
44,
270-281.
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PDB codes:
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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
codes are
shown on the right.
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Links
