View source for 7om0


==Structure of Primase-Helicase in SaPI5==
<StructureSection load='7om0' size='340' side='right'caption='[[7om0]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7om0]] 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=7OM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OM0 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]] 3.1&#8491;</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></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=7om0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7om0 OCA], [https://pdbe.org/7om0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7om0 RCSB], [https://www.ebi.ac.uk/pdbsum/7om0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7om0 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7om0" 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]]