1rlr

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(New page: 200px<br /><applet load="1rlr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlr, resolution 2.5&Aring;" /> '''STRUCTURE OF RIBONUCL...)
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Revision as of 23:34, 20 November 2007

Image:1rlr.jpg

1rlr, resolution 2.5Å

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STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1

Overview

Ribonucleotide reductase is the only enzyme that catalyses de novo, formation of deoxyribonucleotides and is thus a key enzyme in DNA, synthesis. The radical-based reaction involves five cysteins. Two, redox-active cysteines are located at adjacent antiparallel strands in a, new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl, end in a flexible arm. The fifth cysteine, in a loop in the centre of the, barrel, is positioned to initiate the radical reaction.

About this Structure

1RLR is a Single protein structure of sequence from Escherichia coli. Active as Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1 Full crystallographic information is available from OCA.

Reference

Structure of ribonucleotide reductase protein R1., Uhlin U, Eklund H, Nature. 1994 Aug 18;370(6490):533-9. PMID:8052308

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