Journal:IUCrJ:S2052252518018274

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D A cytosine modification mechanism revealed by the ternary complex structure of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate Si Hoon Park, Se Won Suh and Hyun Hyu Song Molecular Tour Crystal structure of the ternary complex of dCMP hydroxylmethylase from bacteriophage T4 (T4dCH) bound with dCMP and tetrahydrofolate was determined at 1.9 Å resolution. The key residues within T4dCH for accommodating a cofactor without the C-terminal tail, an optimized network of ordered water molecules, and hydrophobic gating mechanism for cofactor regulation were clearly identified. Close up view substrate, dCMP and cofactor, tetrahydrofolate. THF (orange) and dCMP (green) are drawn as ball and stick models. Oxygen and nitrogen atoms are colored red and blue, respectively. The ligand-recognizing residues are drawn as ball and stick models. Ionic and hydrogen interactions are drawn by dashed lines. Water molecules are shown as red balls. dCMP binding site. THF binding site. Ternary complex structure of T4dCH with dCMP and THF. A ribbon diagram showing the ternary complex structure of dimeric T4dCH. The bound dCMP (green) and THF (orange) are drawn using the ball and stick model. PDB references: apo T4dCH (I-SAD phasing), 6a9b; ternary complex (T4dCH–dCMP–THF), 6a9a. References

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky