4r1r
From Proteopedia
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RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI
Overview
BACKGROUND: Ribonucleotide reductase (RNR) is an essential enzyme in DNA, synthesis, catalyzing all de novo synthesis of deoxyribonucleotides. The, enzyme comprises two dimers, termed R1 and R2, and contains the redox, active cysteine residues, Cys462 and Cys225. The reduction of, ribonucleotides to deoxyribonucleotides involves the transfer of free, radicals. The pathway for the radical has previously been suggested from, crystallographic results, and is supported by site-directed mutagenesis, studies. Most RNRs are allosterically regulated through two different, nucleotide-binding sites: one site controls general activity and the other, controls substrate specificity. Our aim has been to crystallographically, demonstrate substrate binding and to locate the two effector-binding, sites. ... [(full description)]
About this Structure
4R1R is a [Protein complex] structure of sequences from [Escherichia coli] with TTP and GDP as [ligands]. Active as [Ribonucleoside-diphosphate reductase], with EC number [1.17.4.1]. Structure known Active Sites: ACA, ACB, ACG, SEE, SEI and SES. Full crystallographic information is available from [OCA].
Reference
Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding., Eriksson M, Uhlin U, Ramaswamy S, Ekberg M, Regnstrom K, Sjoberg BM, Eklund H, Structure. 1997 Aug 15;5(8):1077-92. PMID:9309223
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