1h7b

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Revision as of 17:07, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1h7b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h7b, resolution 2.45Å" /> '''STRUCTURAL BASIS FO...)
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File:1h7b.gif


1h7b, resolution 2.45Å

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STRUCTURAL BASIS FOR ALLOSTERIC SUBSTRATE SPECIFICITY REGULATION IN CLASS III RIBONUCLEOTIDE REDUCTASES, NATIVE NRDD

OverviewOverview

BACKGROUND: The specificity of ribonucleotide reductases (RNRs) toward, their four substrates is governed by the binding of deoxyribonucleoside, triphosphates (dNTPs) to the allosteric specificity site. Similar patterns, in the kinetics of allosteric regulation have been a strong argument for a, common evolutionary origin of the three otherwise widely divergent RNR, classes. Recent structural information settled the case for divergent, evolution; however, the structural basis for transmission of the, allosteric signal is currently poorly understood. A comparative study of, the conformational effects of the binding of different effectors has not, yet been possible; in addition, only one RNR class has been studied., RESULTS: Our presentation of the structures of a class III anaerobic RNR, ... [(full description)]

About this StructureAbout this Structure

1H7B is a [Single protein] structure of sequence from [Bacteriophage t4] with PO4 as [ligand]. Active as [[1]], with EC number [1.17.4.2]. Full crystallographic information is available from [OCA].

ReferenceReference

Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases., Larsson KM, Andersson J, Sjoberg BM, Nordlund P, Logan DT, Structure. 2001 Aug;9(8):739-50. PMID:11587648

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