1xjj
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(New page: 200px<br /><applet load="1xjj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xjj, resolution 1.86Å" /> '''Structural mechanism...) |
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| - | [[Image:1xjj.gif|left|200px]]<br /><applet load="1xjj" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1xjj, resolution 1.86Å" /> | ||
| - | '''Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex'''<br /> | ||
| - | == | + | ==Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex== |
| - | Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides | + | <StructureSection load='1xjj' size='340' side='right'caption='[[1xjj]], [[Resolution|resolution]] 1.86Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1xjj]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XJJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DGT:2-DEOXYGUANOSINE-5-TRIPHOSPHATE'>DGT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjj OCA], [https://pdbe.org/1xjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xjj RCSB], [https://www.ebi.ac.uk/pdbsum/1xjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/O33839_THEMT O33839_THEMT] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xj/1xjj_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xjj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:15475969</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1xjj" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima]] | ||
| + | [[Category: Eliasson R]] | ||
| + | [[Category: Jordan A]] | ||
| + | [[Category: Larsson K-M]] | ||
| + | [[Category: Logan DT]] | ||
| + | [[Category: Nordlund P]] | ||
| + | [[Category: Reichard P]] | ||
Current revision
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dGTP complex
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