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PDBsum entry 2fek

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protein links
Hydrolase PDB id
2fek
Jmol
Contents
Protein chain
147 a.a. *
* Residue conservation analysis
PDB id:
2fek
Name: Hydrolase
Title: Structure of a protein tyrosine phosphatase
Structure: Low molecular weight protein-tyrosine- phosphatase wzb. Chain: a. Engineered: yes
Source: Escherichia coli k12. Organism_taxid: 83333. Strain: k-12. Gene: wzb. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: E.Lescop,C.Jin
Key ref:
E.Lescop et al. (2006). 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. PubMed id: 16651264 DOI: 10.1074/jbc.M601263200
Date:
16-Dec-05     Release date:   09-May-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AAB2  (WZB_ECOLI) -  Low molecular weight protein-tyrosine-phosphatase wzb
Seq:
Struc:
147 a.a.
147 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - 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   4 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M601263200 J Biol Chem 281:19570-19577 (2006)
PubMed id: 16651264  
 
 
The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein-tyrosine phosphatases.
E.Lescop, Y.Hu, H.Xu, W.Hu, J.Chen, B.Xia, C.Jin.
 
  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.
 
  Selected figure(s)  
 
Figure 1.
FIGURE 1. The solution structure of E. coli Wzb. A, stereo view of the ensemble of the 20 representative structures of Wzb. Regular secondary structures are colored in blue and loop regions in red. B, ribbon representation of the Wzb structure with secondary structures labeled. C, ribbon representation of Wzb with a 90° rotation related to B. The figures were generated using MOLMOL (33).
Figure 5.
FIGURE 5. Comparisons of Wzb and BPTP. A, stereo view of the active site shown by the C trace superimposition of Wzb (red) and BPTP (black). For clarity, only the P-loop, loop [2]- [2], and loop [4]- [5] are represented. Side chains in loop [2]- [2] and Tyr^117 (Wzb) and Tyr^131 (BPTP) in loop [4]- [5] are displayed and labeled. B, the electrostatic surfaces of Wzb (left) and BPTP (right) are displayed and residues lining the lower part of the crevice are labeled. The figures were generated using MOLMOL (33).
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 19570-19577) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20724509 S.L.Reckseidler-Zenteno, D.F.Viteri, R.Moore, E.Wong, A.Tuanyok, and D.E.Woods (2010).
Characterization of the type III capsular polysaccharide produced by Burkholderia pseudomallei.
  J Med Microbiol, 59, 1403-1414.  
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
  19652335 H.Huang, G.Hagelueken, C.Whitfield, and J.H.Naismith (2009).
Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 770-772.  
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.  
18761695 S.K.Aoki, J.C.Malinverni, K.Jacoby, B.Thomas, R.Pamma, B.N.Trinh, S.Remers, J.Webb, B.A.Braaten, T.J.Silhavy, and D.A.Low (2008).
Contact-dependent growth inhibition requires the essential outer membrane protein BamA (YaeT) as the receptor and the inner membrane transport protein AcrB.
  Mol Microbiol, 70, 323-340.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.