2bq1

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[[Image:2bq1.gif|left|200px]]
 
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{{Structure
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==Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium==
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|PDB= 2bq1 |SIZE=350|CAPTION= <scene name='initialview01'>2bq1</scene>, resolution 3.99&Aring;
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<StructureSection load='2bq1' size='340' side='right'caption='[[2bq1]], [[Resolution|resolution]] 3.99&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+J'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=DGT:2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE'>DGT</scene>
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<table><tr><td colspan='2'>[[2bq1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BQ1 FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.99&#8491;</td></tr>
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|GENE=
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<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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bq1 OCA], [https://pdbe.org/2bq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2bq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bq1 ProSAT]</span></td></tr>
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</table>
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'''RIBONUCLEOTIDE REDUCTASE CLASS 1B HOLOCOMPLEX R1E,R2F FROM SALMONELLA TYPHIMURIUM'''
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== Function ==
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[https://www.uniprot.org/uniprot/RIR3_SALTY RIR3_SALTY] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/2bq1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bq1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Ribonucleotide reductase is an indispensable enzyme for all cells, since it catalyses the biosynthesis of the precursors necessary for both building and repairing DNA. The ribonucleotide reductase class I enzymes, present in all mammals as well as in many prokaryotes and DNA viruses, are composed mostly of two homodimeric proteins, R1 and R2. The reaction involves long-range radical transfer between the two proteins. Here, we present the first crystal structure of a ribonucleotide reductase R1/R2 holocomplex. The biological relevance of this complex is based on the binding of the R2 C terminus in the hydrophobic cleft of R1, an interaction proven to be crucial for enzyme activity, and by the fact that all conserved amino acid residues in R2 are facing the R1 active sites. We suggest that the asymmetric R1/R2 complex observed in the 4A crystal structure of Salmonella typhimurium ribonucleotide reductase represents an intermediate stage in the reaction cycle, and at the moment of reaction the homodimers transiently form a tight symmetric complex.
Ribonucleotide reductase is an indispensable enzyme for all cells, since it catalyses the biosynthesis of the precursors necessary for both building and repairing DNA. The ribonucleotide reductase class I enzymes, present in all mammals as well as in many prokaryotes and DNA viruses, are composed mostly of two homodimeric proteins, R1 and R2. The reaction involves long-range radical transfer between the two proteins. Here, we present the first crystal structure of a ribonucleotide reductase R1/R2 holocomplex. The biological relevance of this complex is based on the binding of the R2 C terminus in the hydrophobic cleft of R1, an interaction proven to be crucial for enzyme activity, and by the fact that all conserved amino acid residues in R2 are facing the R1 active sites. We suggest that the asymmetric R1/R2 complex observed in the 4A crystal structure of Salmonella typhimurium ribonucleotide reductase represents an intermediate stage in the reaction cycle, and at the moment of reaction the homodimers transiently form a tight symmetric complex.
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==About this Structure==
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The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action.,Uppsten M, Farnegardh M, Domkin V, Uhlin U J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:16631785<ref>PMID:16631785</ref>
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2BQ1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BQ1 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action., Uppsten M, Farnegardh M, Domkin V, Uhlin U, J Mol Biol. 2006 Jun 2;359(2):365-77. Epub 2006 Mar 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16631785 16631785]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2bq1" style="background-color:#fffaf0;"></div>
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[[Category: Ribonucleoside-diphosphate reductase]]
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[[Category: Salmonella typhimurium]]
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[[Category: Domkin, V.]]
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[[Category: Farnegardh, M.]]
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[[Category: Uhlin, U.]]
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[[Category: Uppsten, M.]]
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[[Category: DGT]]
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[[Category: FE]]
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[[Category: MG]]
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[[Category: allosteric enzyme]]
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[[Category: allosteric regulation]]
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[[Category: asymmetric complex]]
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[[Category: atp-binding]]
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[[Category: class 1b]]
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[[Category: dna replication]]
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[[Category: holocomplex]]
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[[Category: iron]]
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[[Category: metal-binding]]
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[[Category: nucleotide-binding]]
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[[Category: oxidoreductase]]
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[[Category: r1]]
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[[Category: r1e]]
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[[Category: r2]]
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[[Category: r2f]]
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[[Category: radical transfer]]
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[[Category: ribonucleotide reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:10 2008''
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==See Also==
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*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Domkin V]]
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[[Category: Farnegardh M]]
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[[Category: Uhlin U]]
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[[Category: Uppsten M]]

Current revision

Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium

PDB ID 2bq1

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