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| | <SX load='6aui' size='340' side='right' viewer='molstar' caption='[[6aui]], [[Resolution|resolution]] 3.30Å' scene=''> | | <SX load='6aui' size='340' side='right' viewer='molstar' caption='[[6aui]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6aui]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AUI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6AUI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aui]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AUI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RRM1, RR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=6aui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aui OCA], [https://pdbe.org/6aui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aui RCSB], [https://www.ebi.ac.uk/pdbsum/6aui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aui ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6aui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aui OCA], [http://pdbe.org/6aui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aui RCSB], [http://www.ebi.ac.uk/pdbsum/6aui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aui ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RIR1_HUMAN RIR1_HUMAN]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. | + | [https://www.uniprot.org/uniprot/RIR1_HUMAN RIR1_HUMAN] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Ribonucleotide reductases (RNRs) convert ribonucleotides into deoxyribonucleotides, a reaction essential for DNA replication and repair. Human RNR requires two subunits for activity, the alpha subunit contains the active site, and the beta subunit houses the radical cofactor. Here, we present a 3.3-A resolution structure by cryo-electron microscopy (EM) of a dATP-inhibited state of human RNR. This structure, which was determined in the presence of substrate CDP and allosteric regulators ATP and dATP, has three alpha2 units arranged in an alpha6 ring. At near-atomic resolution, these data provide insight into the molecular basis for CDP recognition by allosteric specificity effectors dATP/ATP. Additionally, we present lower-resolution EM structures of human alpha6 in the presence of both the anticancer drug clofarabine triphosphate and beta2. Together, these structures support a model for RNR inhibition in which beta2 is excluded from binding in a radical transfer competent position when alpha exists as a stable hexamer.
| + | |
| - | | + | |
| - | 3.3-A resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound.,Brignole EJ, Tsai KL, Chittuluru J, Li H, Aye Y, Penczek PA, Stubbe J, Drennan CL, Asturias F Elife. 2018 Feb 20;7. pii: 31502. doi: 10.7554/eLife.31502. PMID:29460780<ref>PMID:29460780</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6aui" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | | *[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribonucleoside-diphosphate reductase]]
| + | [[Category: Asturias FJ]] |
| - | [[Category: Asturias, F J]] | + | [[Category: Brignole EJ]] |
| - | [[Category: Brignole, E J]] | + | [[Category: Drennan CL]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Penczek PA]] |
| - | [[Category: Penczek, P A]] | + | [[Category: Tsai KL]] |
| - | [[Category: Tsai, K L]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ribonucleotide reductase electron transfer radical chemistry thiyl radical]]
| + | |
