7w1f: Difference between revisions

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-'''Unreleased structure'''
-The entry 7w1f is ON HOLD  until Paper Publication
+==Crystal structure of the dNTP triphosphohydrolase PA1124 from Pseudomonas aeruginosa==
+<StructureSection load='7w1f' size='340' side='right'caption='[[7w1f]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7w1f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W1F 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]] 2.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=7w1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w1f OCA], [https://pdbe.org/7w1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w1f RCSB], [https://www.ebi.ac.uk/pdbsum/7w1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w1f ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DGTP_PSEAE DGTP_PSEAE] dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.[HAMAP-Rule:MF_00030]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+dNTP triphosphohydrolase (TPH) belongs to the histidine/aspartate (HD) superfamily and catalyzes the hydrolysis of dNTPs into 2'-deoxyribonucleoside and inorganic triphosphate. TPHs are required for cellular dNTP homeostasis and DNA replication fidelity and are employed as a host defense mechanism. PA1124 from the pathogenic Pseudomonas aeruginosa bacterium functions as a dGTP and dTTP triphosphohydrolase. To reveal how PA1124 drives dNTP hydrolysis and is regulated, we performed a structural study of PA1124. PA1124 assembles into a hexameric architecture as a trimer of dimers. Each monomer has an interdomain dent where a metal ion is coordinated by conserved histidine and aspartate residues. A structure-based comparative analysis suggests that PA1124 accommodates the dNTP substrate into the interdomain dent near the metal ion. Interestingly, PA1124 interacts with ssDNA, presumably as an allosteric regulator, using a positively charged intersubunit cleft that is generated via dimerization. Furthermore, our phylogenetic analysis highlights similar or distinct oligomerization profiles across the TPH family.
-Authors:
+Structural analysis of the dNTP triphosphohydrolase PA1124 from Pseudomonas aeruginosa.,Oh HB, Lee KC, Park SC, Song WS, Yoon SI Biochem Biophys Res Commun. 2022 Jan 22;589:78-84. doi:, 10.1016/j.bbrc.2021.12.002. Epub 2021 Dec 2. PMID:34894560<ref>PMID:34894560</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7w1f" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pseudomonas aeruginosa]]
+[[Category: Lee KC]]
+[[Category: Oh HB]]
+[[Category: Park SC]]
+[[Category: Song WS]]
+[[Category: Yoon SI]]