Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase

Lu, Yi; LaCroix, Louis B.; Lowery, Michael D.; Solomon, Edward I.; Bender, Christopher J.; Peisach, Jack; Roe, James A.; Gralla, Edith Butler; Valentine, Joan Selverstone

doi:10.1021/ja00067a003

Cited by 112 publications

(146 citation statements)

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“…This would indicate subtle differences in the two Cua sites with respect to the strength of this interaction. Similar differences have been well documented for cupredoxins [14][15][16] and it has been shown that 1H NMR of the Cu(II) forms of these proteins is a very sensitive indicator of the strength of this interaction [10,16]. Another possibility is that the extra resonances present in this region of the spectrum of the CUA domain are due to the C ~ protons of the two bridging Cys ligands.…”

Section: Resultssupporting

confidence: 75%

¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase

et al. 1996

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Section: Resultssupporting

confidence: 75%

¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase

et al. 1996

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“…An ~-oxygen/Trp'~ ring face interaction, by contrast, would be electrostatically unfavorable. The distorted tetrahedral geometry of the copper binding site of CST is consistent with the rhombic nature of its EPR spectrum and the band at 450 nm in its visible absorption spectrum (Lu et al, 1993;Andrew et al, 1994). Figure 3 illustrates the copper and its ligands superimposed on 1.6 8, electron density for this region.…”

Section: Copper Binding Sitesupporting

confidence: 64%

A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution

et al. 1996

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Stellacyanins are blue (type I) copper glycoproteins that differ from other members of the cupredoxin family in their spectroscopic and electron transfer properties. Until now, stellacyanins have eluded structure determination. Here we report the three-dimensional crystal structure of the 109 amino acid, non-glycosylated copper binding domain of recombinant cucumber stellacyanin refined to 1.6 8, resolution. The crystallographic R-value for all 18,488 reflections ((T > 0) between 50-1.6 8, is 0.195. The overall fold is organized in two P-sheets, both with four P-strands. Two cy-helices are found in loop regions between P-strands. The P-sheets form a P-sandwich similar to those found in other cupredoxins, but some features differ from proteins such as plastocyanin and azurin in that the P-barrel is more flattened, there is an extra N-terminal a-helix, and the copper binding site is much more solvent accessible. The presence of a disulfide bond at the copper binding end of the protein confirms that cucumber stellacyanin has a phytocyanin-like fold. The ligands to copper are two histidines, one cysteine, and one glutamine, the latter replacing the methionine typically found in mononuclear blue copper proteins. The Cu-Gln bond is one of the shortest axial ligand bond distances observed to date in structurally characterized type I copper proteins. The characteristic spectroscopic properties and electron transfer reactivity of stellacyanin, which differ significantly from those of other well-characterized cupredoxins, can be explained by its more exposed copper site, its distinctive amino acid ligand composition, and its nearly tetrahedral ligand geometry. Surface features on the cucumber stellacyanin molecule that could be involved in interactions with putative redox partners are discussed.

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“…fALS mutant yeast CuZnSOD genes were created by site-directed mutagenesis on pBSIIKS(-)-SODO.5 (12). For expression of SOD in yeast, pBSIIKS(+)-SOD1.1Ncol (13) was digested with EcoRI/BamHI to generate a 1.1-kb fragment containing the wild-type CuZnSOD gene with an Nco I site at the translation start site.…”

mentioning

confidence: 99%

“…CuZnSOD mutants were prepared as described (12). Briefly, pBluescript II KS(-) (Stratagene) containing the SOD gene served as the template for oligonucleotide-directed mutagenesis (18).…”

mentioning

confidence: 99%

Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.

Nishida

Gralla

Valentine

1994

Proc. Natl. Acad. Sci. U.S.A.

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Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase

Cited by 112 publications

References 1 publication

¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase

¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase

A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution

Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.

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Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase

Cited by 112 publications

References 1 publication

1H NMR studies of the paramagnetic CuA center of cytochrome oxidase

1H NMR studies of the paramagnetic CuA center of cytochrome oxidase

A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution

Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.

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¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase

¹H NMR studies of the paramagnetic Cu_A center of cytochrome oxidase