1XRI

X-ray structure of a putative phosphoprotein phosphatase from Arabidopsis thaliana gene AT1G05000

1XRI の概要

• エントリーDOI: 10.2210/pdb1xri/pdb
• 分子名称: At1g05000, SULFATE ION (3 entities in total)
• 機能のキーワード: structural genomics, protein structure initiative, psi, cesg, center for eukaryotic structural genomics, at1g05000, phosphoprotein phosphatase, unknown function
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35464.15

構造登録者

Wesenberg, G.E.,Smith, D.W.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2004-10-14, 公開日: 2004-10-26, 最終更新日: 2024-10-16)

主引用文献

Aceti, D.J.,Bitto, E.,Yakunin, A.F.,Proudfoot, M.,Bingman, C.A.,Frederick, R.O.,Sreenath, H.K.,Vojtik, F.C.,Wrobel, R.L.,Fox, B.G.,Markley, J.L.,Phillips Jr., G.N.
Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000.
Proteins, 73:241-253, 2008

PubMed Abstract: The crystal structure of the protein product of the gene locus At1g05000, a hypothetical protein from A. thaliana, was determined by the multiple-wavelength anomalous diffraction method and was refined to an R factor of 20.4% (R(free) = 24.9%) at 3.3 A. The protein adopts the alpha/beta fold found in cysteine phosphatases, a superfamily of phosphatases that possess a catalytic cysteine and form a covalent thiol-phosphate intermediate during the catalytic cycle. In At1g05000, the analogous cysteine (Cys(150)) is located at the bottom of a positively-charged pocket formed by residues that include the conserved arginine (Arg(156)) of the signature active site motif, HCxxGxxRT. Of 74 model phosphatase substrates tested, purified recombinant At1g05000 showed highest activity toward polyphosphate (poly-P(12-13)) and deoxyribo- and ribonucleoside triphosphates, and less activity toward phosphoenolpyruvate, phosphotyrosine, phosphotyrosine-containing peptides, and phosphatidyl inositols. Divalent metal cations were not required for activity and had little effect on the reaction.

PubMed: 18433060
DOI: 10.1002/prot.22041

実験手法

X-RAY DIFFRACTION (3.3 Å)