|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2oie' size='340' side='right'caption='[[2oie]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2oie' size='340' side='right'caption='[[2oie]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2oie]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OIE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2oie]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OIE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2oig|2oig]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2oie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oie OCA], [https://pdbe.org/2oie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oie RCSB], [https://www.ebi.ac.uk/pdbsum/2oie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oie ProSAT]</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=2oie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oie OCA], [https://pdbe.org/2oie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oie RCSB], [https://www.ebi.ac.uk/pdbsum/2oie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oie ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DCTP1_MOUSE DCTP1_MOUSE]] Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.<ref>PMID:17320107</ref> <ref>PMID:19220460</ref>
| + | [https://www.uniprot.org/uniprot/DCTP1_MOUSE DCTP1_MOUSE] Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.<ref>PMID:17320107</ref> <ref>PMID:19220460</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 34: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Bartlam, M]] | + | [[Category: Bartlam M]] |
| - | [[Category: Chen, W]] | + | [[Category: Chen W]] |
| - | [[Category: Liao, S]] | + | [[Category: Liao S]] |
| - | [[Category: Liu, Y]] | + | [[Category: Liu Y]] |
| - | [[Category: Rao, Z]] | + | [[Category: Rao Z]] |
| - | [[Category: Wu, B]] | + | [[Category: Wu B]] |
| - | [[Category: Zhang, J]] | + | [[Category: Zhang J]] |
| - | [[Category: Zhao, Q]] | + | [[Category: Zhao Q]] |
| - | [[Category: Helix]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
DCTP1_MOUSE Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
RS21-C6, which is highly expressed in all vertebrate genomes and green plants, is proposed to have nucleoside triphosphate pyrophosphohydrolase activity. Here, we report the crystal structures of the core fragment of RS21-C6, named RSCUT, and the complex with the substrate 5-methyl dCTP. The refined structure of RSCUT consists mainly of alpha-helices and shows formation of a tightly associated tetramer. On the basis of the structure of the RSCUT-m5dCTP complex and the results of pyrophosphatase activity assays, several key residues involved in the substrate binding of RS21-C6 have been identified. Tetramer formation is shown to be required for substrate binding.
Crystal structure of RS21-C6, involved in nucleoside triphosphate pyrophosphohydrolysis.,Wu B, Liu Y, Zhao Q, Liao S, Zhang J, Bartlam M, Chen W, Rao Z J Mol Biol. 2007 Apr 13;367(5):1405-12. Epub 2007 Jan 26. PMID:17320107[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wu B, Liu Y, Zhao Q, Liao S, Zhang J, Bartlam M, Chen W, Rao Z. Crystal structure of RS21-C6, involved in nucleoside triphosphate pyrophosphohydrolysis. J Mol Biol. 2007 Apr 13;367(5):1405-12. Epub 2007 Jan 26. PMID:17320107 doi:10.1016/j.jmb.2007.01.057
- ↑ Nonaka M, Tsuchimoto D, Sakumi K, Nakabeppu Y. Mouse RS21-C6 is a mammalian 2'-deoxycytidine 5'-triphosphate pyrophosphohydrolase that prefers 5-iodocytosine. FEBS J. 2009 Mar;276(6):1654-66. doi: 10.1111/j.1742-4658.2009.06898.x. Epub 2009, Feb 7. PMID:19220460 doi:http://dx.doi.org/10.1111/j.1742-4658.2009.06898.x
- ↑ Wu B, Liu Y, Zhao Q, Liao S, Zhang J, Bartlam M, Chen W, Rao Z. Crystal structure of RS21-C6, involved in nucleoside triphosphate pyrophosphohydrolysis. J Mol Biol. 2007 Apr 13;367(5):1405-12. Epub 2007 Jan 26. PMID:17320107 doi:10.1016/j.jmb.2007.01.057
|
