2J16

Apo & Sulphate bound forms of SDP-1

2J16 の概要

• エントリーDOI: 10.2210/pdb2j16/pdb
• 関連するPDBエントリー: 2J17
• 分子名称: TYROSINE-PROTEIN PHOSPHATASE YIL113W, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, protein phosphatase, hypothetical protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42084.50

構造登録者

Briggs, D.C.,McDonald, N.Q. (登録日: 2006-08-09, 公開日: 2007-05-22, 最終更新日: 2024-11-13)

主引用文献

Fox, G.C.,Shafiq, M.,Briggs, D.C.,Knowles, P.P.,Collister, M.,Didmon, M.J.,Makrantoni, V.,Dickinson, R.J.,Hanrahan, S.,Totty, N.,Stark, M.J.,Keyse, S.M.,McDonald, N.Q.
Redox-mediated substrate recognition by Sdp1 defines a new group of tyrosine phosphatases.
Nature, 447:487-492, 2007

PubMed Abstract: Reactive oxygen species trigger cellular responses by activation of stress-responsive mitogen-activated protein kinase (MAPK) signalling pathways. Reversal of MAPK activation requires the transcriptional induction of specialized cysteine-based phosphatases that mediate MAPK dephosphorylation. Paradoxically, oxidative stresses generally inactivate cysteine-based phosphatases by thiol modification and thus could lead to sustained or uncontrolled MAPK activation. Here we describe how the stress-inducible MAPK phosphatase, Sdp1, presents an unusual solution to this apparent paradox by acquiring enhanced catalytic activity under oxidative conditions. Structural and biochemical evidence reveals that Sdp1 employs an intramolecular disulphide bridge and an invariant histidine side chain to selectively recognize a tyrosine-phosphorylated MAPK substrate. Optimal activity critically requires the disulphide bridge, and thus, to the best of our knowledge, Sdp1 is the first example of a cysteine-dependent phosphatase that couples oxidative stress with substrate recognition. We show that Sdp1, and its paralogue Msg5, have similar properties and belong to a new group of phosphatases unique to yeast and fungal taxa.

PubMed: 17495930
DOI: 10.1038/nature05804

実験手法

X-RAY DIFFRACTION (2.7 Å)