Journal:IUCrJ:S2052252518018274
From Proteopedia
(Difference between revisions)
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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. | 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. | ||
| - | <scene name='80/804516/Cv/6'>Close up view substrate, dCMP and cofactor, tetrahydrofolate</scene>. | + | <scene name='80/804516/Cv/6'>Close up view substrate, dCMP and cofactor, tetrahydrofolate</scene>. 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 thin ball-and-stick models. Ionic and hydrogen interactions are drawn by dashed lines. |
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:08, 24 December 2018
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