Conformation of dCDP Bound to Protein R1 of Escherichia coli Ribonucleotide Reductase

✍ Scribed by P. Allard; S. Kuprin; A. Ehrenberg

• Book ID: 102595893
• Publisher: Elsevier Science
• Year: 1994
• Tongue: English
• Weight: 418 KB
• Volume: 103
• Category: Article
• ISSN: 1064-1866
• DOI: 10.1006/jmrb.1994.1036

✦ Synopsis

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.