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Oxidoreductase
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PDB id
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1hfu
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* Residue conservation analysis
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Enzyme class:
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E.C.1.10.3.2
- Laccase.
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Reaction:
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4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O
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4
×
benzenediol
Bound ligand (Het Group name = )
matches with 72.00% similarity
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+
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O(2)
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=
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4
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benzosemiquinone
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+
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2
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H(2)O
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Cofactor:
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Copper
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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oxidation-reduction process
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1 term
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Biochemical function
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oxidoreductase activity
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5 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
57:333-336
(2001)
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PubMed id:
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Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.
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V.Ducros,
A.M.Brzozowski,
K.S.Wilson,
P.Ostergaard,
P.Schneider,
A.Svendson,
G.J.Davies.
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ABSTRACT
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Laccases (E.C. 1.10.3.2; benzenediol oxygen oxidoreductases) couple the
four-electron reduction of dioxygen to water to four one-electron oxidations of
a reducing substrate. The three-dimensional structure of the 'blue' multi-copper
oxidase laccase from the fungus Coprinus cinereus at 1.68 A reveals the
structural basis for isoforms of the type 2 Cu-depleted species.
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Selected figure(s)
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Figure 1.
Figure 1 Cartoon representation of the three-dimensional
structure of the C. cinereus laccase. The figure is
colour-ramped from the N-terminus (blue) to the C-terminus
(red). The Cu atoms are shown as shaded spheres, with the T1
site in blue and the T3 pair in yellow. This figure was produced
using MOLSCRIPT/BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J.
Mol. Graph. 15, 133-138.]; Kraulis, 1991[Kraulis, P. J. (1991).
J. Appl. Cryst. 24, 946-950.]) and rendered using Raster3D
(Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997).
Methods Enzymol. 277, 505-524.]; Merritt & Murphy, 1994[Merritt,
E. A. & Murphy, M. E. P. (1994). Acta Cryst. D50, 869-873.]).
The figure is in divergent (wall-eyed) stereo.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
333-336)
copyright 2001.
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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.B.Rajasekaran,
S.Nilapwar,
S.C.Andrews,
and
K.A.Watson
(2010).
EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport.
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Biometals, 23,
1.
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C.Pezzella,
F.Autore,
P.Giardina,
A.Piscitelli,
G.Sannia,
and
V.Faraco
(2009).
The Pleurotus ostreatus laccase multi-gene family: isolation and heterologous expression of new family members.
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Curr Genet, 55,
45-57.
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J.Yoon,
S.Fujii,
and
E.I.Solomon
(2009).
Geometric and electronic structure differences between the type 3 copper sites of the multicopper oxidases and hemocyanin/tyrosinase.
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Proc Natl Acad Sci U S A, 106,
6585-6590.
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O.V.Morozova,
G.P.Shumakovich,
M.A.Gorbacheva,
S.V.Shleev,
and
A.I.Yaropolov
(2007).
"Blue" laccases.
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Biochemistry (Mosc), 72,
1136-1150.
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T.Skálová,
J.Dohnálek,
L.H.Ostergaard,
P.R.Ostergaard,
P.Kolenko,
J.Dusková,
and
J.Hasek
(2007).
Crystallization and preliminary X-ray diffraction analysis of the small laccase from Streptomyces coelicolor.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 63,
1077-1079.
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Y.Z.Hong,
H.M.Zhou,
X.M.Tu,
J.F.Li,
and
Y.Z.Xiao
(2007).
Cloning of a laccase gene from a novel basidiomycete Trametes sp. 420 and its heterologous expression in Pichia pastoris.
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Curr Microbiol, 54,
260-265.
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A.V.Lyashenko,
I.Bento,
V.N.Zaitsev,
N.E.Zhukhlistova,
Y.N.Zhukova,
A.G.Gabdoulkhakov,
E.Y.Morgunova,
W.Voelter,
G.S.Kachalova,
E.V.Stepanova,
O.V.Koroleva,
V.S.Lamzin,
V.I.Tishkov,
C.Betzel,
P.F.Lindley,
and
A.M.Mikhailov
(2006).
X-ray structural studies of the fungal laccase from Cerrena maxima.
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J Biol Inorg Chem, 11,
963-973.
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A.V.Lyashenko,
N.E.Zhukhlistova,
A.G.Gabdoulkhakov,
Y.N.Zhukova,
W.Voelter,
V.N.Zaitsev,
I.Bento,
E.V.Stepanova,
G.S.Kachalova,
O.V.Koroleva,
E.A.Cherkashyn,
V.I.Tishkov,
V.S.Lamzin,
K.Schirwitz,
E.Y.Morgunova,
C.Betzel,
P.F.Lindley,
and
A.M.Mikhailov
(2006).
Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 62,
954-957.
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PDB code:
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P.Durão,
I.Bento,
A.T.Fernandes,
E.P.Melo,
P.F.Lindley,
and
L.O.Martins
(2006).
Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies.
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J Biol Inorg Chem, 11,
514-526.
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I.Bento,
L.O.Martins,
G.Gato Lopes,
M.Arménia Carrondo,
and
P.F.Lindley
(2005).
Dioxygen reduction by multi-copper oxidases; a structural perspective.
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Dalton Trans, 0,
3507-3513.
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PDB codes:
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N.Hakulinen,
L.L.Kiiskinen,
K.Kruus,
M.Saloheimo,
A.Paananen,
A.Koivula,
and
J.Rouvinen
(2002).
Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site.
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Nat Struct Biol, 9,
601-605.
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PDB code:
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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
code is
shown on the right.
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