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 [1]
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 ֳ… 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.
References
- ↑ Park SH, Suh SW, Song HK. A cytosine modification mechanism revealed by the structure of a ternary complex of deoxycytidylate hydroxymethylase from bacteriophage T4 with its cofactor and substrate. IUCrJ. 2019 Jan 24;6(Pt 2):206-217. doi: 10.1107/S2052252518018274. eCollection, 2019 Mar 1. PMID:30867918 doi:http://dx.doi.org/10.1107/S2052252518018274