7ola: Difference between revisions
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==Structure of Primase-Helicase in SaPI5== | ==Structure of Primase-Helicase in SaPI5== | ||
<StructureSection load='7ola' size='340' side='right'caption='[[7ola]]' scene=''> | <StructureSection load='7ola' size='340' side='right'caption='[[7ola]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OLA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ola]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OLA FirstGlance]. <br> | ||
</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=7ola FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ola OCA], [https://pdbe.org/7ola PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ola RCSB], [https://www.ebi.ac.uk/pdbsum/7ola PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ola ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7ola FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ola OCA], [https://pdbe.org/7ola PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ola RCSB], [https://www.ebi.ac.uk/pdbsum/7ola PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ola ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Replication is a crucial cellular process. Replicative helicases unwind DNA providing the template strand to the polymerase and promoting replication fork progression. Helicases are multi-domain proteins which use an ATPase domain to couple ATP hydrolysis with translocation, however the role that the other domains might have during translocation remains elusive. Here, we studied the unexplored self-loading helicases called Reps, present in Staphylococcus aureus pathogenicity islands (SaPIs). Our cryoEM structures of the PriRep5 from SaPI5 (3.3 A), the Rep1 from SaPI1 (3.9 A) and Rep1-DNA complex (3.1A) showed that in both Reps, the C-terminal domain (CTD) undergoes two distinct movements respect the ATPase domain. We experimentally demonstrate both in vitro and in vivo that SaPI-encoded Reps need key amino acids involved in the staircase mechanism of translocation. Additionally, we demonstrate that the CTD's presence is necessary for the maintenance of full ATPase and helicase activities. We speculate that this high interdomain flexibility couples Rep's activities as initiators and as helicases. | |||
Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.,Qiao C, Debiasi-Anders G, Mir-Sanchis I Nucleic Acids Res. 2022 Jul 25. pii: 6649372. doi: 10.1093/nar/gkac625. PMID:35871290<ref>PMID:35871290</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ola" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mir-Sanchis I]] | [[Category: Mir-Sanchis, I]] | ||
[[Category: Qiao | [[Category: Qiao, C C]] | ||
[[Category: Amppnp]] | |||
[[Category: Dna binding]] | |||
[[Category: Helicase]] | |||
[[Category: Replication]] | |||
Revision as of 08:08, 10 August 2022
Structure of Primase-Helicase in SaPI5Structure of Primase-Helicase in SaPI5
Structural highlights
Publication Abstract from PubMedReplication is a crucial cellular process. Replicative helicases unwind DNA providing the template strand to the polymerase and promoting replication fork progression. Helicases are multi-domain proteins which use an ATPase domain to couple ATP hydrolysis with translocation, however the role that the other domains might have during translocation remains elusive. Here, we studied the unexplored self-loading helicases called Reps, present in Staphylococcus aureus pathogenicity islands (SaPIs). Our cryoEM structures of the PriRep5 from SaPI5 (3.3 A), the Rep1 from SaPI1 (3.9 A) and Rep1-DNA complex (3.1A) showed that in both Reps, the C-terminal domain (CTD) undergoes two distinct movements respect the ATPase domain. We experimentally demonstrate both in vitro and in vivo that SaPI-encoded Reps need key amino acids involved in the staircase mechanism of translocation. Additionally, we demonstrate that the CTD's presence is necessary for the maintenance of full ATPase and helicase activities. We speculate that this high interdomain flexibility couples Rep's activities as initiators and as helicases. Staphylococcal self-loading helicases couple the staircase mechanism with inter domain high flexibility.,Qiao C, Debiasi-Anders G, Mir-Sanchis I Nucleic Acids Res. 2022 Jul 25. pii: 6649372. doi: 10.1093/nar/gkac625. PMID:35871290[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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