PDBsum entry: 1hfu

Oxidoreductase

PDB-id

1hfu

Contents

Description

Header details

Protein chain

Ligands

MAN-MAN

NAG-NDG

Metal ions

_CU ×3

Waters ×461

* Residue conservation analysis

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PDB id:

1hfu

Name:

Oxidoreductase

Title:

Type-2 cu-depleted laccase from coprinus cinereus at 1.68 a resolution

Structure:

Laccase 1. Chain: a. Engineered: yes

Source:

Coprinus cinereus. Inky cap fungus. Organism_taxid: 5346. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062.

UniProt:

Q9Y780 (Q9Y780_COPCI)

Seq:

Struc:

Seq:

Struc:

Seq:

539 a.a.

Struc:

500 a.a.*

Key:		PfamA domain
		Secondary structure			CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme class:

E.C.1.10.3.2 [IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O (see diagram below)

Cofactor:

Copper

Resolution:

1.68Å

R-factor:

0.184

R-free:

0.207

Authors:

V.Ducros,A.M.Brzozowski,G.J.Davies

Key ref:

V.Ducros et al. (2001). Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.. Acta Crystallogr D Biol Crystallogr, 57, 333-336. [PubMed id: 11173497] [DOI: 10.1107/S0907444900013779]

Date:

08-Dec-00

Release date:

06-Dec-01

Related entries:

1a65 type-2 cu-depleted laccase from coprinus cinereus

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Clefts

Surface

Enzyme reaction for E.C.1.10.3.2

4 × benzenediol	+	O(2)	=	4 × benzosemiquinone	+	2 × H(2)O

Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Key reference

DOI no: 10.1107/S0907444900013779 Acta Crystallogr D Biol Crystallogr 57:333-336 (2001)

PubMed id: 11173497

Structure of the laccase from Coprinus cinereus at 1.68 A resolution: evidence for different 'type 2 Cu-depleted' isoforms.

V.Ducros, A.M.Brzozowski, K.S.Wilson, P.Ostergaard, P.Schneider, A.Svendson, G.J.Davies.

ABSTRACT

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.

Selected figure(s)

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.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 333-336) copyright 2001.

Figure was selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id Reference

19034452 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.

Curr Genet, 55, 45-57.

19346471 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.

Proc Natl Acad Sci U S A, 106, 6585-6590.

18021071 O.V.Morozova, G.P.Shumakovich, M.A.Gorbacheva, S.V.Shleev, and A.I.Yaropolov (2007).
"Blue" laccases.

Biochemistry (Mosc), 72, 1136-1150.

17334840 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.

Curr Microbiol, 54, 260-265.

16944230 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.

J Biol Inorg Chem, 11, 963-973.

17012782 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.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 954-957.

PDB code: 2h5u

16680453 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.

J Biol Inorg Chem, 11, 514-526.

16234932 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.

Dalton Trans, 0, 3507-3513.

PDB codes: 1w6l 1w6w 1w8e 2bhf

12118243 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.

Nat Struct Biol, 9, 601-605.

PDB code: 1gw0

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.