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| | <StructureSection load='5im3' size='340' side='right'caption='[[5im3]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5im3' size='340' side='right'caption='[[5im3]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5im3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IM3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IM3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5im3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IM3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">X-ray diffraction, [[Resolution|Resolution]] 2.298Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrdA, PA1156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5im3 OCA], [https://pdbe.org/5im3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5im3 RCSB], [https://www.ebi.ac.uk/pdbsum/5im3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5im3 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=5im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5im3 OCA], [http://pdbe.org/5im3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5im3 RCSB], [http://www.ebi.ac.uk/pdbsum/5im3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5im3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9I4I1_PSEAE Q9I4I1_PSEAE]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410] | + | [https://www.uniprot.org/uniprot/Q9I4I1_PSEAE Q9I4I1_PSEAE] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Ribonucleoside-diphosphate reductase]]
| + | [[Category: Johansson R]] |
| - | [[Category: Johansson, R]] | + | [[Category: Logan DT]] |
| - | [[Category: Logan, D T]] | + | |
| - | [[Category: Allosteric regulation]]
| + | |
| - | [[Category: Atp cone]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ten-stranded alpha-beta barrel]]
| + | |
| Structural highlights
Function
Q9I4I1_PSEAE Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410]
Publication Abstract from PubMed
Ribonucleotide reductases (RNRs) reduce ribonucleotides to deoxyribonucleotides. Their overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures. The crystal structure and solution X-ray scattering data of a novel dATP-induced homotetramer of the Pseudomonas aeruginosa class I RNR reveal the structural bases for its unique properties, namely one ATP cone that binds two dATP molecules and a second one that is non-functional, binding no nucleotides. Mutations in the observed tetramer interface ablate oligomerization and dATP-induced inhibition but not the ability to bind dATP. Sequence analysis shows that the novel type of ATP cone may be widespread in RNRs. The present study supports a scenario in which diverse mechanisms for allosteric activity regulation are gained and lost through acquisition and evolutionary erosion of different types of ATP cone.
Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.,Johansson R, Jonna VR, Kumar R, Nayeri N, Lundin D, Sjoberg BM, Hofer A, Logan DT Structure. 2016 Apr 27. pii: S0969-2126(16)30036-3. doi:, 10.1016/j.str.2016.03.025. PMID:27133024[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Johansson R, Jonna VR, Kumar R, Nayeri N, Lundin D, Sjoberg BM, Hofer A, Logan DT. Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones. Structure. 2016 Apr 27. pii: S0969-2126(16)30036-3. doi:, 10.1016/j.str.2016.03.025. PMID:27133024 doi:http://dx.doi.org/10.1016/j.str.2016.03.025
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