5VJW

Arabidopsis thaliana Rhizobiales-like phosphatase 2 complexed with tungstate

5VJW の概要

• エントリーDOI: 10.2210/pdb5vjw/pdb
• 関連するPDBエントリー: 5VJV
• 分子名称: Rhizobiales-like phosphatase 2, ZINC ION, TUNGSTATE(VI)ION, ... (4 entities in total)
• 機能のキーワード: protein phosphorylation, arabidopsis thaliana, phosphoprotein phosphatase, protein phosphatase, protein tyrosine phosphatase, tungstate, hydrolase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35102.49

構造登録者

Ng, K.K.S.,Labandera, A.,Moorhead, G. (登録日: 2017-04-20, 公開日: 2018-03-21, 最終更新日: 2024-03-13)

主引用文献

Labandera, A.M.,Uhrig, R.G.,Colville, K.,Moorhead, G.B.,Ng, K.K.S.
Structural basis for the preference of the Arabidopsis thalianaphosphatase RLPH2 for tyrosine-phosphorylated substrates.
Sci Signal, 11:-, 2018

PubMed Abstract: Despite belonging to the phosphoserine- and phosphothreonine-specific phosphoprotein phosphatase (PPP) family, -like phosphatase 2 (RLPH2) strongly prefers substrates bearing phosphorylated tyrosine residues. We solved the structures of RLPH2 crystallized in the presence or absence of sodium tungstate. These structures revealed the presence of a central domain that forms a binding site for two divalent metal ions that closely resembles that of other PPP-family enzymes. Unique structural elements from two flanking domains suggest a mechanism for the selective dephosphorylation of phosphotyrosine residues. Cocrystallization with the phosphate mimetic tungstate also suggests how positively charged residues that are highly conserved in the RLPH2 class form an additional pocket that is specific for a phosphothreonine residue located near the phosphotyrosine residue that is bound to the active site. Site-directed mutagenesis confirmed that this auxiliary recognition element facilitates the recruitment of dual-phosphorylated substrates containing a pTxpY motif.

PubMed: 29615518
DOI: 10.1126/scisignal.aan8804

実験手法

X-RAY DIFFRACTION (1.8 Å)