2FEK
Structure of a protein tyrosine phosphatase
Summary for 2FEK
| Entry DOI | 10.2210/pdb2fek/pdb |
| NMR Information | BMRB: 6934 |
| Descriptor | Low molecular weight protein-tyrosine-phosphatase wzb (1 entity in total) |
| Functional Keywords | low molecular weight protein tyrosine phosphatase, escherichia coli, phosphate binding, hydrolase |
| Biological source | Escherichia coli K12 |
| Total number of polymer chains | 1 |
| Total formula weight | 18904.68 |
| Authors | Lescop, E.,Jin, C. (deposition date: 2005-12-16, release date: 2006-05-09, Last modification date: 2024-05-29) |
| Primary citation | Lescop, E.,Hu, Y.,Xu, H.,Hu, W.,Chen, J.,Xia, B.,Jin, C. 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, 2006 Cited by PubMed 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. PubMed: 16651264DOI: 10.1074/jbc.M601263200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
