YjeF N terminal protein domain

At the cellular level, the YjeF-N terminal domain is vital to the assembly of the processing body (P-body). This aids mRNA decay and is thought to bring together different complexes to aggregate mRNPs.[1] At the organism level, in bacteria and archaea, YjeF N-terminal domains are often fused to a YjeF C-terminal domain with high structural homology to the members of a ribokinase-like superfamily or belong to operons that encode enzymes of diverse functions. Examples of such include:

• pyridoxal phosphate biosynthetic protein PdxJ;
• phosphopanteine-protein transferase;
• ATP/GTP hydrolase;
• and pyruvate-formate lyase 1-activating enzyme.

In plants, the YjeF N-terminal domain is fused to a C-terminal putative pyridoxamine 5'-phosphate oxidase. In eukaryotes, proteins that consist of (Sm)-FDF-YjeF N-terminal domains may be involved in RNA processing.[2][3]

The YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature. The YjeF N-terminal domain is a three-layer alpha-beta-alpha sandwich with a central beta-sheet surrounded by alpha helices. The conservation of the acidic residues in the predicted active site of the YjeF N-terminal domains shows some similarities to the amino acids found in the active sites of diverse hydrolases.[2][3]