Figure 1.

The ePK catalytic domain. The 12 conserved subdomains are indicated by Roman numerals. The positions of amino-acid residues and motifs highly conserved throughout the ePK superfamily are indicated above the subdomains, using the single-letter amino-acid code with x as any amino acid. Crystal structures show that ePK domains adopt a common fold consisting of amino-terminal and carboxy-terminal lobes connected by a hinge region. Binding of Mg-ATP is largely the function of the amino-terminal lobe and hinge region, while peptide-substrate binding is mediated by the carboxy-terminal lobe. Particularly important for catalytic function are the invariant lysine in subdomain II and the invariant aspartate in subdomain VII that function to anchor and orient ATP, and the invariant aspartate in subdomain VIB which is the likely catalytic base in the phosphotransfer reaction. More detailed discussions of ePK subdomains and conserved residues in relation to crystal structures and catalytic function can be found in [3,4,12,13].

Hanks Genome Biology 2003 4:111   doi:10.1186/gb-2003-4-5-111