Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 Å resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases (original) (raw)

2007, Proteins: Structure, Function, and Bioinformatics

Protein phosphorylation-dephosphorylation is a universal mechanism used to regulate protein function. Historically, research efforts have focused on protein kinases, but recently the role of phosphatases that catalyze the equally important dephosphorylation step is becoming increasingly appreciated. 1 The role of protein phosphorylation in eukaryotic signal transduction is well documented. Among bacteria, protein phosphatases such as Yersinia pestis YopH are virulence factors, which are secreted into human cells during pathogenic invasion. However, recent genomic studies have identified numerous protein phosphatase homologs in nonpathogenic bacteria, suggesting intrinsic function within these organisms. Despite their ancient origin, which possibly predates the eukaryote/prokaryote split, and the resulting sequence and structural divergence, all known protein tyrosine phosphatases (PTPs) have a canonical functional motif consisting of Cys-(X) 5 -Arg. This motif is part of a