1JER

CUCUMBER STELLACYANIN, CU2+, PH 7.0

1JER の概要

• エントリーDOI: 10.2210/pdb1jer/pdb
• 分子名称: CUCUMBER STELLACYANIN, COPPER (II) ION (3 entities in total)
• 機能のキーワード: electron transport, copper, glycoprotein, hydroxylation
• 由来する生物種: Cucumis sativus (cucumber)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14953.08

構造登録者

Hart, P.J.,Nersissian, A.M.,Herrmann, R.G.,Nalbandyan, R.M.,Valentine, J.S.,Eisenberg, D. (登録日: 1996-08-21, 公開日: 1997-02-12, 最終更新日: 2024-10-30)

主引用文献

Hart, P.J.,Nersissian, A.M.,Herrmann, R.G.,Nalbandyan, R.M.,Valentine, J.S.,Eisenberg, D.
A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 A resolution.
Protein Sci., 5:2175-2183, 1996

PubMed Abstract: 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 A resolution. The crystallographic R-value for all 18,488 reflections (sigma > 0) between 50-1.6 A is 0.195. The overall fold is organized in two beta-sheets, both with four beta-stands. Two alpha-helices are found in loop regions between beta-strands. The beta-sheets form a beta-sandwich similar to those found in other cupredoxins, but some features differ from proteins such as plastocyanin and azurin in that the beta-barrel is more flattened, there is an extra N-terminal alpha-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.

PubMed: 8931136

実験手法

X-RAY DIFFRACTION (1.6 Å)