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'''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1''' | '''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1''' | ||
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[[Category: Eklund, H.]] | [[Category: Eklund, H.]] | ||
[[Category: Uhlin, U.]] | [[Category: Uhlin, U.]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
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Revision as of 04:39, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 07:39:09 2008