PDBsum entry: 2fek

Hydrolase

PDB id: 2fek

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

Protein chain

P0AAB2  (WZB_ECOLI) -  Low molecular weight protein-tyrosine-phosphatase wzb

Seq: 147 a.a.

Struc: 147 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: polysaccharide biosynthetic process (2 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.