A crystallographic model for azurin at 3 Å resolution

Adman, Elinor T.; Stenkamp, Ronald E.; Sieker, L.C.; Jensen, L. H.

doi:10.1016/0022-2836(78)90375-3

Cited by 365 publications

(155 citation statements)

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“…Each subunit of the dimer is divided into three domains with a similar polypeptide folding of a P-barrel type. The domains are thus clearly related to the small coppercontaining blue proteins such as plastocyanins of plants (Colman et al, 1978) and azurins of bacteria (Adman et al, 1978). Therefore it would seem probable that the AOase has evolved through a triplication of an ancestral gene coding for a small copper protein (Messerschmidt et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

“…The type 1 copper configuration is clearly homologous to the only copper atom in the small copper proteins (Colman et al, 1978;Adman et al, 1978). The ligands for this copper (two His, Met and Cys) that lie in the C-terminal domain 3 are conserved in the fungal laccases with one exception : Met 519 of the AOase is replaced by a leucine or a phenylalanine.…”

Section: Kfqingvtfvpptvpvllqilsgaqsaadllpsgsvyalpsnatielslpag-----mentioning

confidence: 99%

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Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Saloheimo

Niku‐Paavola

Knowles

1991

Journal of General Microbiology

127

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We have isolated and characterized a gene coding for the laccase of the lignin-degrading fungus Phlebia radiaftr, The gene has nine introns and recognizable fungal promoter elements. Sequences homologous to the consensus eukaryotic heat-shock regulatory element can be found in the promoter. RNA hybridization results indicate that this gene is regulated at the transcriptional level. The derived laccase amino acid sequence shows homology to plant ascorbate oxidases, suggesting that the basic structure of the laccase is similar to the three-fold repeated P-barrel of the ascorbate oxidases. Potential copper ligands and a residue carrying the prosthetic group pyrroloquinoline quinone (PQQ) in the laccase protein can be identified by homology. The intron/exon structure of the laccase gene suggests that this protein could have evolved by exon shuffiing.

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Section: Discussionmentioning

confidence: 99%

Section: Kfqingvtfvpptvpvllqilsgaqsaadllpsgsvyalpsnatielslpag-----mentioning

confidence: 99%

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Saloheimo

Niku‐Paavola

Knowles

1991

Journal of General Microbiology

127

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“…Significant advances in the molecular biology of mononuclear copper proteins have taken place in recent years, particularly for plastocyanin and azurin, both of which were structurally characterized by X-ray crystallography in 1978 (Adman et al, 1978;Colman et al, 1978). The first nucleotide sequences of genes encoding mononuclear blue copper proteins were determined for plastocyanins from Spinaciu olerucea and Silene prutensis (Smeekens et al, 1985;Rother et al, 1986).…”

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Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

et al. 1996

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The cDNA encoding the 182 amino acid long precursor stellacyanin from Cucumis sariwus was isolated and characterized. The protein precursor consists of four sequence domains: I, a 23 amino acid hydrophobic N-terminal signal peptide with features characteristic of secretory proteins; 11, a 109 amino acid copper-binding domain; 111, a 26 amino acid hydroxyproline-and serine-rich peptide characteristic of motifs found in the extensin family, extracellular structural glycoproteins found in plant cell walls; and IV, a 22 amino acid hydrophobic extension. Maturation of the protein involves posttranslational processing of domains I and IV. The copper-binding domain (domain 11), which shares high sequence identity with other stellacyanins, has been expressed without its carbohydrate attachment sites, refolded from the Escherichia coli inclusion bodies, purified, and characterized by electronic absorption, EPR, ESEEM, and RR spectroscopy. Its spectroscopic properties are nearly identical to those of stellacyanin from the Japanese lacquer tree Rhus verniciferu, the most extensively studied and best characterized stellacyanin, indicating that this domain folds correctly, even in the absence of its carbohydrate moiety. The presence of a hydroxyproline-and serine-rich domain I11 suggests that stellacyanin may have a function other than that of a diffusible electron transfer protein, conceivably participating in redox reactions localized at the plant cell wall, which are known to occur in response to wounding or infection of the plant.

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“…Resonances associated with the single tryptophan residue, all six phenylalanine residues, one of the two tyrosine residues and all four histidine residues, as well as most of the resonances from the ring-current shifted methyl groups have been assigned. These assignments have been used to study the pH dependence of the structure of the protein and binding of analogues of redox-active reagents to the protein.With the advent of the crystal structures of two 'blue' copper proteins, azurin [1,2] and plastocyanin [3], it has been possible to interpret many of the spectroscopic properties of these intriguing proteins [4]. Most attention has been paid to the metal ion and its immediate environment.…”

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The assignment of the ¹H nuclear magnetic resonance spectrum of azurin

Canters¹,

Hill²,

Kitchen³

et al. 1984

European Journal of Biochemistry

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A detailed assignment of the 'H nuclear magnetic resonance spectrum of azurin has been made. Resonances associated with the single tryptophan residue, all six phenylalanine residues, one of the two tyrosine residues and all four histidine residues, as well as most of the resonances from the ring-current shifted methyl groups have been assigned. These assignments have been used to study the pH dependence of the structure of the protein and binding of analogues of redox-active reagents to the protein.With the advent of the crystal structures of two 'blue' copper proteins, azurin [1,2] and plastocyanin [3], it has been possible to interpret many of the spectroscopic properties of these intriguing proteins [4]. Most attention has been paid to the metal ion and its immediate environment. A high level of consistency between the crystallographic and spectroscopic investigations is apparent, though the detailed nature of the interaction of the putative methionine ligand with the copper is still somewhat obscure [3,5]. There is evidence that the coordination site is sensitive to the oxidation state of the copper, to the pH of the solution or crystal and to the temperature [6 -81.The proteins are of interest, not only for the structural features they embody, but also because of the role they play in bacterial and photosynthetic electron transfer [3]. The 'substrates' of redox proteins are the proteins with which they interact. To date, there have been no detailed investigations of the structures of protein-protein complexes, though there have been many careful studies of the kinetics and mechanism of inter-protein electron transfer [7 -91. The same is true of their reactions with redox agents of low relative molecular mass [lo-131. There is evidence that both of these classes of reactions proceed via the formation of precursor complexes. With azurin, in particular, there is additional interest in its structure and function because of its possible relationship to segments of other copper-containing proteins such as cytochrome oxidase and caeruloplasmin.Nuclear magnetic resonance spectroscopy is of value in revealing both the features of the structure and the dynamics associated with them. There have been a number of NMR investigations of plastocyanin and azurin This paper is dedicated to the memory of Eraldo Antonini. Abbreviations. COSY, 'H -'H correlated spectroscopy; NMR, nuclear magnetic resonance; NOE, nuclear Overhauser effect ; ppm, parts per million; SEDR, spin-echo double resonance spectroscopy, 1 D and 2D, one-dimensional and two-dimensional; pH* and pK*, values of pH and pK obtained from direct meter readings without correction for the deuterium isotope effect; phen (in complexes), 1 ,lo-phenanthroline. resonances were assigned but, lacking the crystal structure, only distinctive resonances, such as those associated with histidine residues, could be readily exploited. The availability of the crystal structure and the advent of more powerful pulse sequences has extended the application of H NMR spectroscopy to ...

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A crystallographic model for azurin at 3 Å resolution

Cited by 365 publications

References 30 publications

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

The assignment of the ¹H nuclear magnetic resonance spectrum of azurin

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A crystallographic model for azurin at 3 Å resolution

Cited by 365 publications

References 30 publications

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

The assignment of the 1H nuclear magnetic resonance spectrum of azurin

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The assignment of the ¹H nuclear magnetic resonance spectrum of azurin