8g9f
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8g9f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G9F FirstGlance]. <br> | <table><tr><td colspan='2'>[[8g9f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8G9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G9F FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8g9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g9f OCA], [https://pdbe.org/8g9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g9f RCSB], [https://www.ebi.ac.uk/pdbsum/8g9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g9f 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=8g9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g9f OCA], [https://pdbe.org/8g9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g9f RCSB], [https://www.ebi.ac.uk/pdbsum/8g9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g9f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | The mechanism by which polymerase alpha - primase (polalpha-primase) synthesizes chimeric RNA-DNA primers of defined length and composition, necessary for replication fidelity and genome stability, is unknown. Here, we report cryo-EM structures of polalpha-primase in complex with primed templates representing various stages of DNA synthesis. Our data show how interaction of the primase regulatory subunit with the primer 5' | + | The mechanism by which polymerase alpha-primase (polalpha-primase) synthesizes chimeric RNA-DNA primers of defined length and composition, necessary for replication fidelity and genome stability, is unknown. Here, we report cryo-EM structures of Xenopus laevis polalpha-primase in complex with primed templates representing various stages of DNA synthesis. Our data show how interaction of the primase regulatory subunit with the primer 5' end facilitates handoff of the primer to polalpha and increases polalpha processivity, thereby regulating both RNA and DNA composition. The structures detail how flexibility within the heterotetramer enables synthesis across two active sites and provide evidence that termination of DNA synthesis is facilitated by reduction of polalpha and primase affinities for the varied conformations along the chimeric primer-template duplex. Together, these findings elucidate a critical catalytic step in replication initiation and provide a comprehensive model for primer synthesis by polalpha-primase. |
| - | A mechanistic model of primer synthesis from catalytic structures of DNA polymerase alpha-primase.,Mullins EA, Salay LE, Durie CL, Jackman JE, Ohi MD, Chazin WJ, Eichman BF | + | A mechanistic model of primer synthesis from catalytic structures of DNA polymerase alpha-primase.,Mullins EA, Salay LE, Durie CL, Bradley NP, Jackman JE, Ohi MD, Chazin WJ, Eichman BF Nat Struct Mol Biol. 2024 May;31(5):777-790. doi: 10.1038/s41594-024-01227-4. , Epub 2024 Mar 15. PMID:38491139<ref>PMID:38491139</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 8g9f" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8g9f" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Complete auto-inhibitory complex of Xenopus laevis DNA polymerase alpha-primase
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