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| | <StructureSection load='5c2o' size='340' side='right'caption='[[5c2o]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5c2o' size='340' side='right'caption='[[5c2o]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c2o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Strmu Strmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C2O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c2o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans_UA159 Streptococcus mutans UA159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C2O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5-TRIPHOSPHATE'>TTP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">comEB, SMU_1849 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210007 STRMU])</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=5c2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2o OCA], [https://pdbe.org/5c2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c2o RCSB], [https://www.ebi.ac.uk/pdbsum/5c2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2o ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c2o OCA], [http://pdbe.org/5c2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c2o RCSB], [http://www.ebi.ac.uk/pdbsum/5c2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c2o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8DSE5_STRMU Q8DSE5_STRMU] |
| | <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: Strmu]] | + | [[Category: Streptococcus mutans UA159]] |
| - | [[Category: Dong, Y H]] | + | [[Category: Dong YH]] |
| - | [[Category: Gao, Z Q]] | + | [[Category: Gao ZQ]] |
| - | [[Category: Hou, H F]] | + | [[Category: Hou HF]] |
| - | [[Category: Li, Y H]] | + | [[Category: Li YH]] |
| - | [[Category: Allosteric regulation]]
| + | |
| - | [[Category: Dcmp deaminase]]
| + | |
| - | [[Category: Enzyme complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| Structural highlights
Function
Q8DSE5_STRMU
Publication Abstract from PubMed
In cells, dUMP is the intermediate precursor of dTTP in its synthesis during deoxynucleotide metabolism. In Gram-positive bacteria and eukaryotes, zinc-dependent deoxycytidylate deaminases (dCDs) catalyze the conversion of dCMP to dUMP. The activity of dCD is allosterically activated by dCTP and inhibited by dTTP. Here, the crystal structure of Streptococcus mutans dCD (SmdCD) complexed with dTTP is presented at 2.35 A resolution, thereby solving the first pair of activator-bound and inhibitor-bound structures from the same species to provide a more definitive description of the allosteric mechanism. In contrast to the dTTP-bound dCD from the bacteriophage S-TIM5 (S-TIM5-dCD), dTTP-bound SmdCD adopts an inactive conformation similar to the apo form. A structural comparison suggests that the distinct orientations of the triphosphate group in S-TIM5-dCD and SmdCD are a result of the varying protein binding environment. In addition, calorimetric data establish that the modulators bound to dCD can be mutually competitively replaced. The results reveal the mechanism underlying its regulator-specific activity and might greatly enhance the understanding of the allosteric regulation of other dCDs.
Mechanism of the allosteric regulation of Streptococcus mutans 2'-deoxycytidylate deaminase.,Li Y, Guo Z, Jin L, Wang D, Gao Z, Su X, Hou H, Dong Y Acta Crystallogr D Struct Biol. 2016 Jul;72(Pt 7):883-91. doi:, 10.1107/S2059798316009153. Epub 2016 Jun 23. PMID:27377385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li Y, Guo Z, Jin L, Wang D, Gao Z, Su X, Hou H, Dong Y. Mechanism of the allosteric regulation of Streptococcus mutans 2'-deoxycytidylate deaminase. Acta Crystallogr D Struct Biol. 2016 Jul;72(Pt 7):883-91. doi:, 10.1107/S2059798316009153. Epub 2016 Jun 23. PMID:27377385 doi:http://dx.doi.org/10.1107/S2059798316009153
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