1xjj

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[[Image:1xjj.gif|left|200px]]<br /><applet load="1xjj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xjj.gif|left|200px]]
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caption="1xjj, resolution 1.86&Aring;" />
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'''Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex'''<br />
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{{Structure
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|PDB= 1xjj |SIZE=350|CAPTION= <scene name='initialview01'>1xjj</scene>, resolution 1.86&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=DGT:2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE'>DGT</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1]
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|GENE= nrdj ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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}}
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'''Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=DGT:'>DGT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJJ OCA].
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1XJJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJJ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15475969 15475969]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15475969 15475969]
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: substrate specificity]]
[[Category: substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:10:41 2008''

Revision as of 13:10, 20 March 2008


PDB ID 1xjj

Drag the structure with the mouse to rotate
, resolution 1.86Å
Ligands: and
Gene: nrdj (Thermotoga maritima)
Activity: Ribonucleoside-diphosphate reductase, with EC number 1.17.4.1
Coordinates: save as pdb, mmCIF, xml



Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex


Overview

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.

About this Structure

1XJJ 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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