1ZGG

Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis

1ZGG の概要

• エントリーDOI: 10.2210/pdb1zgg/pdb
• 分子名称: Putative low molecular weight protein-tyrosine-phosphatase ywlE (1 entity in total)
• 機能のキーワード: alpha/beta, four-stranded parallel beta sheet, structural genomics, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16810.20

構造登録者

Xu, H.,Xia, B.,Jin, C. (登録日: 2005-04-21, 公開日: 2006-03-28, 最終更新日: 2024-05-29)

主引用文献

Xu, H.,Xia, B.,Jin, C.
Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis
J.Bacteriol., 188:1509-1517, 2006

PubMed Abstract: The low-molecular-weight (LMW) protein tyrosine phosphatases (PTPs) exist ubiquitously in prokaryotes and eukaryotes and play important roles in cellular processes. We report here the solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis. YwlE consists of a twisted central four-stranded parallel beta-sheet with seven alpha-helices packing on both sides. Similar to LMW PTPs from other organisms, the conformation of the YwlE active site is favorable for phosphotyrosine binding, indicating that it may share a common catalytic mechanism in the hydrolysis of phosphate on tyrosine residue in proteins. Though the overall structure resembles that of the eukaryotic LMW PTPs, significant differences were observed around the active site. Residue Asp115 is likely interacting with residue Arg13 through electrostatic interaction or hydrogen bond interaction to stabilize the conformation of the active cavity, which may be a unique character of bacterial LMW PTPs. Residues in the loop region from Phe40 to Thr48 forming a wall of the active cavity are more flexible than those in other regions. Ala41 and Gly45 are located near the active cavity and form a noncharged surface around it. These unique properties demonstrate that this loop may be involved in interaction with specific substrates. In addition, the results from spin relaxation experiments elucidate further insights into the mobility of the active site. The solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial LMW PTPs.

PubMed: 16452434
DOI: 10.1128/JB.188.4.1509-1517.2006

実験手法

SOLUTION NMR