Journal:IUCrJ:S2052252518018274

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<StructureSection load='' size='450' side='right' scene='80/804516/Cv/1' caption='80/804516/Cv/1'>
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<StructureSection load='' size='450' side='right' scene='80/804516/Cv/1' caption=''>
===A cytosine modification mechanism revealed by the ternary complex structure of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate===
===A cytosine modification mechanism revealed by the ternary complex structure of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate===
<big>Si Hoon Park, Se Won Suh and Hyun Hyu Song</big> <ref>doi 10.1107/S2052252518018274</ref>
<big>Si Hoon Park, Se Won Suh and Hyun Hyu Song</big> <ref>doi 10.1107/S2052252518018274</ref>
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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.
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<scene name='80/804516/Cv/6'>Close up view substrate, dCMP and cofactor, tetrahydrofolate</scene>.
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<scene name='80/804516/Cv/18'>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 ball and stick models. Ionic and hydrogen interactions are drawn by dashed lines. Water molecules are shown as red balls.
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*<scene name='80/804516/Cv/19'>dCMP binding site</scene>.
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*<scene name='80/804516/Cv/20'>THF binding site</scene>.
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<scene name='80/804516/Cv/23'>Ternary complex structure of T4dCH with dCMP and THF</scene>. 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.
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'''PDB references:''' apo T4dCH (I-SAD phasing), [[6a9b]]; ternary complex (T4dCH–dCMP–THF), [[6a9a]].
<b>References</b><br>
<b>References</b><br>

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