2FEK

Structure of a protein tyrosine phosphatase

2FEK の概要

• エントリーDOI: 10.2210/pdb2fek/pdb
• NMR情報: BMRB: 6934
• 分子名称: Low molecular weight protein-tyrosine-phosphatase wzb (1 entity in total)
• 機能のキーワード: low molecular weight protein tyrosine phosphatase, escherichia coli, phosphate binding, hydrolase
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18904.68

構造登録者

Lescop, E.,Jin, C. (登録日: 2005-12-16, 公開日: 2006-05-09, 最終更新日: 2024-05-29)

主引用文献

Lescop, E.,Hu, Y.,Xu, H.,Hu, W.,Chen, J.,Xia, B.,Jin, C.
The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases
J.Biol.Chem., 281:19570-19577, 2006

PubMed Abstract: Low molecular weight protein-tyrosine phosphatases (LMW-PTPs) are small enzymes that ubiquitously exist in various organisms and play important roles in many biological processes. In Escherichia coli, the LMW-PTP Wzb dephosphorylates the autokinase Wzc, and the Wzc/Wzb pair regulates colanic acid production. However, the substrate recognition mechanism of Wzb is still poorly understood thus far. To elucidate the molecular basis of the catalytic mechanism, we have determined the solution structure of Wzb at high resolution by NMR spectroscopy. The Wzb structure highly resembles that of the typical LMW-PTP fold, suggesting that Wzb may adopt a similar catalytic mechanism with other LMW-PTPs. Nevertheless, in comparison with eukaryotic LMW-PTPs, the absence of an aromatic amino acid at the bottom of the active site significantly alters the molecular surface and implicates Wzb may adopt a novel substrate recognition mechanism. Furthermore, a structure-based multiple sequence alignment suggests that a class of the prokaryotic LMW-PTPs may share a similar substrate recognition mechanism with Wzb. The current studies provide the structural basis for rational drug design against the pathogenic bacteria.

PubMed: 16651264
DOI: 10.1074/jbc.M601263200

実験手法

SOLUTION NMR