7tu3

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<StructureSection load='7tu3' size='340' side='right'caption='[[7tu3]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
<StructureSection load='7tu3' size='340' side='right'caption='[[7tu3]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7tu3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TU3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7tu3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Leeuwenhoekiella_blandensis_MED217 Leeuwenhoekiella blandensis MED217]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TU3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=7tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tu3 OCA], [https://pdbe.org/7tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/7tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tu3 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=7tu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tu3 OCA], [https://pdbe.org/7tu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tu3 RCSB], [https://www.ebi.ac.uk/pdbsum/7tu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tu3 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/A3XHN1_LEEBM A3XHN1_LEEBM]]
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Deoxynucleoside triphosphate (dNTP) triphosphohydrolases (dNTPases) are important enzymes that may perform multiple functions in the cell, including regulating the dNTP pools and contributing to innate immunity against viruses. Among the homologs that are best studied are human SAMHD1, a tetrameric dNTPase, and the hexameric E. coli dGTPase; however, it is unclear whether these are representative of all dNTPases given their wide distribution throughout life. Here, we investigated a hexameric homolog from the marine bacterium Leeuwenhoekiella blandensis, revealing that it is a dGTPase that is subject to allosteric activation by dATP, specifically. Allosteric regulation mediated solely by dATP represents a novel regulatory feature among dNTPases that may facilitate maintenance of cellular dNTP pools in L. blandensis. We present high-resolution X-ray crystallographic structures (1.80-2.26 A) in catalytically important conformations as well as cryo-EM structures (2.1-2.7 A) of the enzyme bound to dGTP and dATP ligands. The structures, the highest resolution cryo-EM structures of any SAMHD1-like dNTPase to date, reveal an intact metal-binding site with the dGTP substrate coordinated to three metal ions. These structural and biochemical data yield insights into the catalytic mechanism and support a conserved catalytic mechanism for the tetrameric and hexameric dNTPase homologs. We conclude that the allosteric activation by dATP appears to rely on structural connectivity between the allosteric and active sites, as opposed to the changes in oligomeric state upon ligand binding used by SAMHD1.
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High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.,Klemm BP, Sikkema AP, Hsu AL, Horng JC, Hall TMT, Borgnia MJ, Schaaper RM J Biol Chem. 2022 May 25:102073. doi: 10.1016/j.jbc.2022.102073. PMID:35643313<ref>PMID:35643313</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7tu3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hall, T M.T]]
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[[Category: Leeuwenhoekiella blandensis MED217]]
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[[Category: Horng, J C]]
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[[Category: Hall TMT]]
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[[Category: Klemm, B P]]
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[[Category: Horng JC]]
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[[Category: Sikkema, A P]]
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[[Category: Klemm BP]]
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[[Category: Dgtpase]]
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[[Category: Sikkema AP]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide binding]]
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Revision as of 05:30, 8 September 2022

Structure of the L. blandensis dGTPase del55-58 mutant

PDB ID 7tu3

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