1xjg

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[[Image:1xjg.gif|left|200px]]
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{{Seed}}
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[[Image:1xjg.png|left|200px]]
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{{STRUCTURE_1xjg| PDB=1xjg | SCENE= }}
{{STRUCTURE_1xjg| PDB=1xjg | SCENE= }}
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'''Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex'''
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===Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex===
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==Overview==
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Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides into deoxyribonucleotides, which constitute the precursor pools used for DNA synthesis and repair. Imbalances in these pools increase mutational rates and are detrimental to the cell. Balanced precursor pools are maintained primarily through the regulation of the RNR substrate specificity. Here, the molecular mechanism of the allosteric substrate specificity regulation is revealed through the structures of a dimeric coenzyme B12-dependent RNR from Thermotoga maritima, both in complexes with four effector-substrate nucleotide pairs and in three complexes with only effector. The mechanism is based on the flexibility of loop 2, a key structural element, which forms a bridge between the specificity effector and substrate nucleotides. Substrate specificity is achieved as different effectors and their cognate substrates stabilize specific discrete loop 2 conformations. The mechanism of substrate specificity regulation is probably general for most class I and class II RNRs.
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The line below this paragraph, {{ABSTRACT_PUBMED_15475969}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15475969 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15475969}}
==About this Structure==
==About this Structure==
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[[Category: Ribonucleotide reductase]]
[[Category: Ribonucleotide reductase]]
[[Category: Substrate specificity]]
[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:06:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:58:08 2008''

Revision as of 09:58, 27 July 2008

Image:1xjg.png

Template:STRUCTURE 1xjg

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex

Template:ABSTRACT PUBMED 15475969

About this Structure

1XJG is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase., Larsson KM, Jordan A, Eliasson R, Reichard P, Logan DT, Nordlund P, Nat Struct Mol Biol. 2004 Nov;11(11):1142-9. Epub 2004 Oct 10. PMID:15475969

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