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. 2015 Sep 30;79(4):419–435. doi: 10.1128/MMBR.00038-15

FIG 2.

FIG 2

PII protein structure. (A) PII trimer. The binding sites for MgATP (magenta) and 2-OG (black) at the lateral clefts between each subunit are indicated. (B) Closer view of the 2-OG binding site. 2-OG interacts with the side chains of conserved lysine (K58) and glutamine (Q39) residues (green sticks) and also with MgATP. 2-OG binding affects the PII T-loop structure, thereby altering the affinity between PII and its binding protein targets. In proteobacteria, the structure of the T loop is also influenced by reversible uridylylation at the conserved tyrosine residue indicated (Y51). The figure was prepared using Pymol and PDB entry 3MHY.