PDBsum entry 1zgg

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protein links
Hydrolase PDB id
Protein chain
150 a.a. *
* Residue conservation analysis
PDB id:
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
21-Apr-05     Release date:   28-Mar-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P39155  (YWLE_BACSU) -  Low molecular weight protein-tyrosine-phosphatase YwlE
150 a.a.
150 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     peptidyl-tyrosine dephosphorylation   2 terms 
  Biochemical function     hydrolase activity     3 terms  


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.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19616007 G.Hagelueken, H.Huang, I.L.Mainprize, C.Whitfield, and J.H.Naismith (2009).
Crystal structures of Wzb of Escherichia coli and CpsB of Streptococcus pneumoniae, representatives of two families of tyrosine phosphatases that regulate capsule assembly.
  J Mol Biol, 392, 678-688.
PDB codes: 2wja 2wjd 2wje 2wjf
19678837 J.Blobel, P.Bernadó, H.Xu, C.Jin, and M.Pons (2009).
Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria.
  FEBS J, 276, 4346-4357.  
18298793 L.Tabernero, A.R.Aricescu, E.Y.Jones, and S.E.Szedlacsek (2008).
Protein tyrosine phosphatases: structure-function relationships.
  FEBS J, 275, 867-882.  
17008719 D.Tolkatchev, R.Shaykhutdinov, P.Xu, J.Plamondon, D.C.Watson, N.M.Young, and F.Ni (2006).
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.
  Protein Sci, 15, 2381-2394.
PDB code: 2gi4
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