Isoaspartyl dipeptidase (IadA) is an enzyme that catalyzes the hydrolysis of an isoaspartyl dipeptide-like moiety, which can be inappropriately formed in proteins, between the β-carboxyl group side chain of Asp and the amino group of the following amino acid. Here, we have determined the structures of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea, both ligand-free and that...

background: vasopressin type 2 receptor (v2r) plays an important role in the water reabsorption in the kidney collecting ducts. v2r is a g protein coupled receptor (gpcr) and the triplet of amino acids aspartate-arginine-histidine (drh) in this receptor might significantly influence its activity similar to other gpcr. however, the role of this motif has not been fully confirmed. therefore, the ...

Class I PI3K are heterodimers composed of a p85 regulatory subunit and p110 catalytic involved in multiple cellular functions. Recently, the p110β has emerged as class isoform playing major role tumorigenesis. Understanding its regulation is crucial for control pathway p110β-driven cancers. Here we sought to evaluate putative by SUMO. Our data show that can be modified SUMO1 SUMO2 vitro, transf...

A hybrid protein that comprises the beta-lactamase signal peptide fused precisely to chicken muscle triosephosphate isomerase is not secreted into the periplasm of Escherichia coli. The protein can be secreted, however, if an arginine residue at position 3 of the isomerase is replaced by either a serine or a proline residue. In contrast, replacement of a neighboring lysine residue has no effect...

Figure 1 Model of two independent PTMs, serine-pyrophosphorylation and lysine-polyphosphorylation Protein pyrophosphorylation is the transfer of the b-phosphate group of the pyrophosphate moiety of IP7 on to a pre-phosphorylated serine residue (left) [16,17]. Conversely, protein polyphosphorylation is the covalent attachment of a chain of inorganic polyP on to a lysine residue dependent on the ...

Introduction: Non-enzymatic glycation of proteins has been implicated in various diabetic complications and age-related disorders. Proteins undergo glycation at the N-terminus or at the O-amino group of lysine residues. The observation that only a fraction of all lysine residues undergo glycation indicates the role of the immediate chemical environment in the glycation reaction. Here we have co...

INTRODUCTION Non-enzymatic glycation of proteins has been implicated in various diabetic complications and age-related disorders. Proteins undergo glycation at the N-terminus or at the epsilon-amino group of lysine residues. The observation that only a fraction of all lysine residues undergo glycation indicates the role of the immediate chemical environment in the glycation reaction. Here we ha...

ParB proteins are one of the three essential components of partition systems that actively segregate bacterial chromosomes and plasmids. In binding to centromere sequences, ParB assembles as nucleoprotein structures called partition complexes. These assemblies are the substrates for the partitioning process that ensures DNA molecules are segregated to both sides of the cell. We recently identif...