1b5e
DCMP HYDROXYMETHYLASE FROM T4
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OverviewOverview
Bacteriophage T4 deoxycytidylate hydroxymethylase (EC 2.1.2.8), a, homodimer of 246-residue subunits, catalyzes hydroxymethylation of the, cytosine base in deoxycytidylate (dCMP) to produce 5-hydroxymethyl-dCMP., It forms part of a phage DNA protection system and appears to function in, vivo as a component of a multienzyme complex called deoxyribonucleoside, triphosphate (dNTP) synthetase. We have determined its crystal structure, in the presence of the substrate dCMP at 1.6 A resolution. The structure, reveals a subunit fold and a dimerization pattern in common with, thymidylate synthases, despite low (approximately 20%) sequence identity., Among the residues that form the dCMP binding site, those interacting with, the sugar and phosphate are arranged in a configuration similar to the, ... [(full description)]
About this StructureAbout this Structure
1B5E is a [Single protein] structure of sequence from [Enterobacteria phage t2] with DCM as [ligand]. Active as [Deoxycytidylate 5-hydroxymethyltransferase], with EC number [2.1.2.8]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of deoxycytidylate hydroxymethylase from bacteriophage T4, a component of the deoxyribonucleoside triphosphate-synthesizing complex., Song HK, Sohn SH, Suh SW, EMBO J. 1999 Mar 1;18(5):1104-13. PMID:10064578
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