9ln0
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==A thermostable enzyme dUTPase P45== | |
| + | <StructureSection load='9ln0' size='340' side='right'caption='[[9ln0]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9ln0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LN0 FirstGlance]. <br> | ||
| + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ln0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ln0 OCA], [https://pdbe.org/9ln0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ln0 RCSB], [https://www.ebi.ac.uk/pdbsum/9ln0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ln0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DCD_PYRFU DCD_PYRFU] Catalyzes the deamination of dCTP to dUTP. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | dUTPase is a critical enzyme responsible for hydrolyzing dUTP to dUMP and pyrophosphate (PPi), thereby maintaining genomic integrity by preventing uracil misincorporation into DNA. P45, an archaeal dUTPase, enhances polymerase chain reaction (PCR) efficiency by increasing product yield and amplification duration. However, its oligomeric state and catalytic mechanism remain poorly characterized. Here, we report the crystal structures of Pyrococcus furiosus P45 in its apo form (P45-apo) and in complex with dUMP (P45-dUMP) at 2.1 A and 2.2 A resolution. Mutational studies identified key residues (W93, D95, T103, Y138) essential for enzymatic activity. Comparative structural analysis revealed that P45 shares a highly conserved catalytic core with trimeric dUTPases across diverse species, including archaea, bacteria, eukaryotes, viruses, and protozoa. Substrate binding induced conformational rearrangements, stabilizing beta-sheet formation and active site closure. These findings elucidate the structural basis of P45's thermostability and PCR-enhancing activity, providing insights for its application in high-fidelity DNA amplification systems. | ||
| - | + | Structural and functional characterization of thermostable dUTPase P45 from Pyrococcus furiosus with enhanced PCR efficiency.,Dong B, Li J, Zhang L, Zhang B, Xu B, Ye S, Wang Y Int J Biol Macromol. 2025 Aug;320(Pt 3):146110. doi: , 10.1016/j.ijbiomac.2025.146110. Epub 2025 Jul 16. PMID:40680961<ref>PMID:40680961</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9ln0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pyrococcus furiosus DSM 3638]] | ||
| + | [[Category: Dong BJ]] | ||
| + | [[Category: Wang YX]] | ||
Current revision
A thermostable enzyme dUTPase P45
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