7ola: Difference between revisions
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==Structure of Primase-Helicase in SaPI5== | |||
<StructureSection load='7ola' size='340' side='right'caption='[[7ola]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ola]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1S5ZIL8_STAAU A0A1S5ZIL8_STAAU] | |||
<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 Aug 12;50(14):8349-8362. 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ola" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus]] | |||
[[Category: Mir-Sanchis I]] | |||
[[Category: Qiao CC]] | |||
Latest revision as of 12:01, 14 July 2024
Structure of Primase-Helicase in SaPI5Structure of Primase-Helicase in SaPI5
Structural highlights
FunctionPublication 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 Aug 12;50(14):8349-8362. doi: 10.1093/nar/gkac625. PMID:35871290[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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