1rlr: Difference between revisions

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[[Image:1rlr.jpg|left|200px]]
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{{STRUCTURE_1rlr|  PDB=1rlr  |  SCENE=  }}  
{{STRUCTURE_1rlr|  PDB=1rlr  |  SCENE=  }}  


'''STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1'''
===STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8052308}}


==About this Structure==
==About this Structure==
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[[Category: Uhlin, U.]]
[[Category: Uhlin, U.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:39:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:34:30 2008''

Revision as of 21:34, 28 July 2008

File:1rlr.png

Template:STRUCTURE 1rlr

STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1

Template:ABSTRACT PUBMED 8052308

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

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