Conformation of dCDP bound to protein R1 of Escherichia coli ribonucleotide reductase.
Deoxycytidine 5'-diphosphate (dCDP) is a product and competitive inhibitor of ribonucleoside-diphosphate reductase (EC 1.17.4.1) from Escherichia coli. Its conformation in the enzyme-bound state is of importance for understanding the reaction mechanism. Free and bound dCDP are in fast exchange and the transferred nuclear Overhauser effect in two-dimensional 1H NMR was used to obtain information about interproton distances within bound dCDP. The results are consistent with a model of dCDP with the base in anti conformation and the sugar in S-type puckering, when bound either to the complete enzyme complex or to the large protein subunit alone.
Department of Biophysics, Stockholm University, Sweden.
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Allard
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Kuprin
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Ehrenberg
D003845:Deoxycytosine Nucleotides / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D012262:Ribonucleoside Diphosphate Reductase / Q000737:chemistry*; D012264:Ribonucleotide Reductases / Q000737:chemistry*
D003845:Deoxycytosine Nucleotides; C045813:2'-deoxycytidine diphosphate; D012264:Ribonucleotide Reductases; D012262:Ribonucleoside Diphosphate Reductase