PDBsum entry: 1zgg

Hydrolase

PDB id: 1zgg

Contents

Protein chain

150 a.a. *

* Residue conservation analysis

PDB id:

1zgg

Name:

Hydrolase

Title:

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

Structure:

Putative low molecular weight protein-tyrosine- phosphatase ywle. Chain: a. Synonym: low molecular weight protein tyrosine phosphatase. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

H.Xu,B.Xia,C.Jin

Key ref:

H.Xu et al. (2006). Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis. J Bacteriol, 188, 1509-1517. PubMed id: 16452434 DOI: 10.1128/JB.188.4.1509-1517.2006

Date:

21-Apr-05 Release date: 28-Mar-06

Protein chain

P39155  (YWLE_BACSU) -  Low molecular weight protein-tyrosine-phosphatase ywlE

Seq: 150 a.a.

Struc: 150 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: protein amino acid dephosphorylation (1 term)
• Biochemical function: hydrolase activity (3 terms)

reference

DOI no: 10.1128/JB.188.4.1509-1517.2006

J Bacteriol 188:1509-1517 (2006)

PubMed id: 16452434

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

H.Xu, B.Xia, C.Jin.

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.