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Oxidoreductase PDB-id
1a65
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Contents
Description
Header details
Header records
References
PROCHECK
Protein chain
504 a.a. *
Ligands
NAG
PYE
__O
Metal ions
_CU ×3
Waters ×296

* Residue conservation analysis
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PDB id: 1a65
Name: Oxidoreductase
Title: Type-2 cu-depleted laccase from coprinus cinereus

Structure:
Laccase. Chain: a. Engineered: yes

Source:
Coprinopsis cinerea. Organism_taxid: 5346. Expressed in: aspergillus oryzae. Expression_system_taxid: 5062

UniProt:
Q9Y780 (Q9Y780_COPCI) Pfam  
Seq:
Struc:
Seq:
Struc:
Seq: 539 a.a.
Struc: 505 a.a.*
Key:    PfamA domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

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:
2.23Å

R-factor:
0.160

R-free:
0.220

Authors:
V.Ducros,W.Brzozowski

Key ref:
V.Ducros et al. (1998). Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution.. Nat Struct Biol, 5, 310-316. [PubMed id: 9546223] [DOI: 10.1038/nsb0498-310]

Added 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 no: 10.1107/S0907444900013779]

Date:
05-Mar-98

Release date:
30-Mar-99
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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: 10.1038/nsb0498-310 Nat Struct Biol 5:310-316 (1998)
PubMed id: 9546223  
 
 
Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution.
V.Ducros, A.M.Brzozowski, K.S.Wilson, S.H.Brown, P.Ostergaard, P.Schneider, D.S.Yaver, A.H.Pedersen, G.J.Davies.
 
  ABSTRACT  
 
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 A. Laccase is a monomer composed of three cupredoxin-like beta-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18581264 D.W.Wong (2009).
Structure and action mechanism of ligninolytic enzymes.
  Appl Biochem Biotechnol, 157, 174-209.  
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.  
19360388 K.Hildén, T.K.Hakala, and T.Lundell (2009).
Thermotolerant and thermostable laccases.
  Biotechnol Lett, 31, 1117-1128.  
19780817 M.Andberg, N.Hakulinen, S.Auer, M.Saloheimo, A.Koivula, J.Rouvinen, and K.Kruus (2009).
Essential role of the C-terminus in Melanocarpus albomyces laccase for enzyme production, catalytic properties and structure.
  FEBS J, 276, 6285-6300.  
19282479 S.Ghosh, X.Xie, A.Dey, Y.Sun, C.P.Scholes, and E.I.Solomon (2009).
Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function.
  Proc Natl Acad Sci U S A, 106, 4969-4974.  
19224923 T.J.Lawton, L.A.Sayavedra-Soto, D.J.Arp, and A.C.Rosenzweig (2009).
Crystal structure of a two-domain multicopper oxidase: IMPLICATIONS FOR THE EVOLUTION OF MULTICOPPER BLUE PROTEINS.
  J Biol Chem, 284, 10174-10180.
PDB code: 3g5w
19771344 Y.Shimazaki, M.Takani, and O.Yamauchi (2009).
Metal complexes of amino acids and amino acid side chain groups. Structures and properties.
  Dalton Trans, 0, 7854-7869.  
19221878 Z.Haibo, Z.Yinglong, H.Feng, G.Peiji, and C.Jiachuan (2009).
Purification and characterization of a thermostable laccase with unique oxidative characteristics from Trametes hirsuta.
  Biotechnol Lett, 31, 837-843.  
19019256 A.Kunamneni, S.Camarero, C.García-Burgos, F.J.Plou, A.Ballesteros, and M.Alcalde (2008).
Engineering and Applications of fungal laccases for organic synthesis.
  Microb Cell Fact, 7, 32.  
18443781 G.Bleve, C.Lezzi, G.Mita, P.Rampino, C.Perrotta, L.Villanova, and F.Grieco (2008).
Molecular cloning and heterologous expression of a laccase gene from Pleurotus eryngii in free and immobilized Saccharomyces cerevisiae cells.
  Appl Microbiol Biotechnol, 79, 731-741.  
18292878 M.A.Tadesse, A.D'Annibale, C.Galli, P.Gentili, and F.Sergi (2008).
An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates.
  Org Biomol Chem, 6, 868-878.  
18165683 R.Wiener, Y.Haitin, L.Shamgar, M.C.Fernández-Alonso, A.Martos, O.Chomsky-Hecht, G.Rivas, B.Attali, and J.A.Hirsch (2008).
The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction.
  J Biol Chem, 283, 5815-5830.
PDB code: 3bj4
17897461 M.Ferraroni, N.M.Myasoedova, V.Schmatchenko, A.A.Leontievsky, L.A.Golovleva, A.Scozzafava, and F.Briganti (2007).
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases.
  BMC Struct Biol, 7, 60.
PDB code: 2qt6
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.  
17101662 S.R.Waterman, M.Hacham, J.Panepinto, G.Hu, S.Shin, and P.R.Williamson (2007).
Cell wall targeting of laccase of Cryptococcus neoformans during infection of mice.
  Infect Immun, 75, 714-722.  
16740638 A.Beloqui, M.Pita, J.Polaina, A.Martínez-Arias, O.V.Golyshina, M.Zumárraga, M.M.Yakimov, H.García-Arellano, M.Alcalde, V.M.Fernández, K.Elborough, J.M.Andreu, A.Ballesteros, F.J.Plou, K.N.Timmis, M.Ferrer, and P.N.Golyshin (2006).
Novel polyphenol oxidase mined from a metagenome expression library of bovine rumen: biochemical properties, structural analysis, and phylogenetic relationships.
  J Biol Chem, 281, 22933-22942.  
16317711 A.Marjasvaara, K.Kruus, and P.Vainiotalo (2006).
A laccase study by electrospray ionization Fourier transform ion cyclotron resonance MS: copper depletion, glycoforms and stability.
  J Mass Spectrom, 41, 91-97.  
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
16472305 P.Baldrian (2006).
Fungal laccases - occurrence and properties.
  FEMS Microbiol Rev, 30, 215-242.  
16650005 P.J.Hoegger, S.Kilaru, T.Y.James, J.R.Thacker, and U.Kües (2006).
Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences.
  FEBS J, 273, 2308-2326.  
16775746 S.Kilaru, P.J.Hoegger, and U.Kües (2006).
The laccase multi-gene family in Coprinopsis cinerea has seventeen different members that divide into two distinct subfamilies.
  Curr Genet, 50, 45-60.  
16391148 S.Sakasegawa, H.Ishikawa, S.Imamura, H.Sakuraba, S.Goda, and T.Ohshima (2006).
Bilirubin oxidase activity of Bacillus subtilis CotA.
  Appl Environ Microbiol, 72, 972-975.  
16230618 A.B.Taylor, C.S.Stoj, L.Ziegler, D.J.Kosman, and P.J.Hart (2005).
The copper-iron connection in biology: structure of the metallo-oxidase Fet3p.
  Proc Natl Acad Sci U S A, 102, 15459-15464.
PDB code: 1zpu
16231129 G.Battistuzzi, M.Bellei, A.Leonardi, R.Pierattelli, A.De Candia, A.J.Vila, and M.Sola (2005).
Reduction thermodynamics of the T1 Cu site in plant and fungal laccases.
  J Biol Inorg Chem, 10, 867-873.  
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
16332742 Y.Taprab, T.Johjima, Y.Maeda, S.Moriya, S.Trakulnaleamsai, N.Noparatnaraporn, M.Ohkuma, and T.Kudo (2005).
Symbiotic fungi produce laccases potentially involved in phenol degradation in fungus combs of fungus-growing termites in Thailand.
  Appl Environ Microbiol, 71, 7696-7704.  
15468136 A.Marjasvaara, M.Torvinen, and P.Vainiotalo (2004).
Laccase-catalyzed mediated oxidation of benzyl alcohol: the role of TEMPO and formation of products including benzonitrile studied by nanoelectrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
  J Mass Spectrom, 39, 1139-1146.  
14764581 F.J.Enguita, D.Marçal, L.O.Martins, R.Grenha, A.O.Henriques, P.F.Lindley, and M.A.Carrondo (2004).
Substrate and dioxygen binding to the endospore coat laccase from Bacillus subtilis.
  J Biol Chem, 279, 23472-23476.
PDB codes: 1hkz 1uvw
12637519 F.J.Enguita, L.O.Martins, A.O.Henriques, and M.A.Carrondo (2003).
Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties.
  J Biol Chem, 278, 19416-19425.
PDB code: 1gsk
14532088 L.F.Larrondo, L.Salas, F.Melo, R.Vicuña, and D.Cullen (2003).
A novel extracellular multicopper oxidase from Phanerochaete chrysosporium with ferroxidase activity.
  Appl Environ Microbiol, 69, 6257-6263.  
12800133 S.V.Kumar, P.S.Phale, S.Durani, and P.P.Wangikar (2003).
Combined sequence and structure analysis of the fungal laccase family.
  Biotechnol Bioeng, 83, 386-394.  
12009907 A.E.Palmer, L.Quintanar, S.Severance, T.P.Wang, D.J.Kosman, and E.I.Solomon (2002).
Spectroscopic characterization and O2 reactivity of the trinuclear Cu cluster of mutants of the multicopper oxidase Fet3p.
  Biochemistry, 41, 6438-6448.  
12473107 A.Klonowska, C.Gaudin, A.Fournel, M.Asso, J.Le Petit, M.Giorgi, and T.Tron (2002).
Characterization of a low redox potential laccase from the basidiomycete C30.
  Eur J Biochem, 269, 6119-6125.  
11872481 A.P.Litvintseva, and J.M.Henson (2002).
Cloning, characterization, and transcription of three laccase genes from Gaeumannomyces graminis var. tritici, the take-all fungus.
  Appl Environ Microbiol, 68, 1305-1311.  
11856319 E.Record, P.J.Punt, M.Chamkha, M.Labat, C.A.van Den Hondel, and M.Asther (2002).
Expression of the Pycnoporus cinnabarinus laccase gene in Aspergillus niger and characterization of the recombinant enzyme.
  Eur J Biochem, 269, 602-609.  
12115407 F.Hong, N.Q.Meinander, and L.J.Jönsson (2002).
Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris.
  Biotechnol Bioeng, 79, 438-449.  
12163489 K.Piontek, M.Antorini, and T.Choinowski (2002).
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers.
  J Biol Chem, 277, 37663-37669.
PDB code: 1gyc
11884407 L.O.Martins, C.M.Soares, M.M.Pereira, M.Teixeira, T.Costa, G.H.Jones, and A.O.Henriques (2002).
Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat.
  J Biol Chem, 277, 18849-18859.  
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
12177070 P.Vachette, E.Dainese, V.B.Vasyliev, P.Di Muro, M.Beltramini, D.I.Svergun, V.De Filippis, and B.Salvato (2002).
A key structural role for active site type 3 copper ions in human ceruloplasmin.
  J Biol Chem, 277, 40823-40831.  
11867755 S.A.Roberts, A.Weichsel, G.Grass, K.Thakali, J.T.Hazzard, G.Tollin, C.Rensing, and W.R.Montfort (2002).
Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli.
  Proc Natl Acad Sci U S A, 99, 2766-2771.
PDB code: 1kv7
12044164 T.Bertrand, C.Jolivalt, P.Briozzo, E.Caminade, N.Joly, C.Madzak, and C.Mougin (2002).
Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics.
  Biochemistry, 41, 7325-7333.
PDB code: 1kya
11170402 A.Donaire, B.Jiménez, J.Moratal, J.F.Hall, and S.S.Hasnain (2001).
Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential?
  Biochemistry, 40, 837-846.  
11466290 C.Kim, W.W.Lorenz, J.T.Hoopes, and J.F.Dean (2001).
Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene.
  J Bacteriol, 183, 4866-4875.  
12404359 E.I.Solomon, P.Chen, M.Metz, S.K.Lee, and A.E.Palmer (2001).
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins.
  Angew Chem Int Ed Engl, 40, 4570-4590.  
16233113 H.Hoshida, M.Nakao, H.Kanazawa, K.Kubo, T.Hakukawa, K.Morimasa, R.Akada, and Y.Nishizawa (2001).
Isolation of five laccase gene sequences from the white-rot fungus Trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts.
  J Biosci Bioeng, 92, 372-380.  
10712591 L.Otterbein, E.Record, S.Longhi, M.Asther, and S.Moukha (2000).
Molecular cloning of the cDNA encoding laccase from Pycnoporus cinnabarinus I-937 and expression in Pichia pastoris.
  Eur J Biochem, 267, 1619-1625.  
10642183 M.J.Colaneri, J.Vitali, and J.Peisach (2000).
Electron spin-echo envelope modulation study of multicrystalline Cu(2+)-insulin: effects of Cd(2+) on the nuclear quadrupole interaction of the Cu(2+)-coordinated imidazole remote nitrogen.
  Biochemistry, 39, 584-591.  
10694398 N.J.Blackburn, M.Ralle, R.Hassett, and D.J.Kosman (2000).
Spectroscopic analysis of the trinuclear cluster in the Fet3 protein from yeast, a multinuclear copper oxidase.
  Biochemistry, 39, 2316-2324.  
10839819 U.Kües (2000).
Life history and developmental processes in the basidiomycete Coprinus cinereus.
  Microbiol Mol Biol Rev, 64, 316-353.  
10074356 A.Shimizu, J.H.Kwon, T.Sasaki, T.Satoh, N.Sakurai, T.Sakurai, S.Yamaguchi, and T.Samejima (1999).
Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands.
  Biochemistry, 38, 3034-3042.  
  10543807 D.S.Yaver, M.D.Overjero, F.Xu, B.A.Nelson, K.M.Brown, T.Halkier, S.Bernauer, S.H.Brown, and S.Kauppinen (1999).
Molecular characterization of laccase genes from the basidiomycete Coprinus cinereus and heterologous expression of the laccase lcc1.
  Appl Environ Microbiol, 65, 4943-4948.  
10212209 F.Xu, A.E.Palmer, D.S.Yaver, R.M.Berka, G.A.Gambetta, S.H.Brown, and E.I.Solomon (1999).
Targeted mutations in a Trametes villosa laccase. Axial perturbations of the T1 copper.
  J Biol Chem, 274, 12372-12375.  
  10542175 G.Alexandre, R.Bally, B.L.Taylor, and I.B.Zhulin (1999).
Loss of cytochrome c oxidase activity and acquisition of resistance to quinone analogs in a laccase-positive variant of Azospirillum lipoferum.
  J Bacteriol, 181, 6730-6738.  
10551829 H.Huang, G.Zoppellaro, and T.Sakurai (1999).
Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase.
  J Biol Chem, 274, 32718-32724.  
10583375 I.Gromov, A.Marchesini, O.Farver, I.Pecht, and D.Goldfarb (1999).
Azide binding to the trinuclear copper center in laccase and ascorbate oxidase.
  Eur J Biochem, 266, 820-830.  
12501394 I.Masuda-Nishimura, K.Ichikawa, O.Hatamoto, K.Abe, and Y.Koyama (1999).
cDNA cloning of bilirubin oxidase from Pleurotus ostreatus strain Shinshu and its expression in Aspergillus sojae: an efficient screening of transformants, using the laccase activity of bilirubin oxidase.
  J Gen Appl Microbiol, 45, 93-97.  
  10543802 J.Zhao, and H.S.Kwan (1999).
Characterization, molecular cloning, and differential expression analysis of laccase genes from the edible mushroom Lentinula edodes.
  Appl Environ Microbiol, 65, 4908-4913.  
  10584012 M.Gelo-Pujic, H.H.Kim, N.G.Butlin, and G.T.Palmore (1999).
Electrochemical studies of a truncated laccase produced in Pichia pastoris.
  Appl Environ Microbiol, 65, 5515-5521.  
10473564 O.Farver, L.Bendahl, L.K.Skov, and I.Pecht (1999).
Human ceruloplasmin. Intramolecular electron transfer kinetics and equilibration.
  J Biol Chem, 274, 26135-26140.  
9649340 T.E.Machonkin, H.H.Zhang, B.Hedman, K.O.Hodgson, and E.I.Solomon (1998).
Spectroscopic and magnetic studies of human ceruloplasmin: identification of a redox-inactive reduced Type 1 copper site.
  Biochemistry, 37, 9570-9578.  
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.

 
    Added 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  
 
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 A. Laccase is a monomer composed of three cupredoxin-like beta-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms.
 
  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.