CONFORMATION OF DCDP BOUND TO PROTEIN-R1 OF ESCHERICHIA-COLI RIBONUCLEOTIDE REDUCTASE

被引：3

作者：

ALLARD, P

KUPRIN, S

EHRENBERG, A

机构：

[1] Department of Biophysics, Stockholm University, Arrhenius Laboratory

来源：

JOURNAL OF MAGNETIC RESONANCE SERIES B | 1994年 / 103卷 / 03期

关键词：

D O I：

10.1006/jmrb.1994.1036

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

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 H-1 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. (C) 1994 Academic Press, Inc.

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页码：242 / 246

页数：5

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