View source for 5yww


==Archael RuvB-like Holiday junction helicase==
<StructureSection load='5yww' size='340' side='right'caption='[[5yww]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_islandicus_REY15A Sulfolobus islandicus REY15A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YWW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5yww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yww OCA], [https://pdbe.org/5yww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yww RCSB], [https://www.ebi.ac.uk/pdbsum/5yww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yww ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0NID4_SULIR F0NID4_SULIR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PINA is a novel ATPase and DNA helicase highly conserved in Archaea, the third domain of life. The PINA from Sulfolobus islandicus (SisPINA) forms a hexameric ring in crystal and solution. The protein is able to promote Holliday junction (HJ) migration and physically and functionally interacts with Hjc, the HJ specific endonuclease. Here, we show that SisPINA has direct physical interaction with Hjm (Hel308a), a helicase presumably targeting replication forks. In vitro biochemical analysis revealed that Hjm, Hjc, and SisPINA are able to coordinate HJ migration and cleavage in a concerted way. Deletion of the carboxyl 13 amino acid residues impaired the interaction between SisPINA and Hjm. Crystal structure analysis showed that the carboxyl 70 amino acid residues fold into a type II KH domain which, in other proteins, functions in binding RNA or ssDNA. The KH domain not only mediates the interactions of PINA with Hjm and Hjc but also regulates the hexameric assembly of PINA. Our results collectively suggest that SisPINA, Hjm and Hjc work together to function in replication fork regression, HJ formation and HJ cleavage.

The archaeal ATPase PINA interacts with the helicase Hjm via its carboxyl terminal KH domain remodeling and processing replication fork and Holliday junction.,Zhai B, DuPrez K, Han X, Yuan Z, Ahmad S, Xu C, Gu L, Ni J, Fan L, Shen Y Nucleic Acids Res. 2018 May 29. pii: 5017765. doi: 10.1093/nar/gky451. PMID:29846688<ref>PMID:29846688</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yww" style="background-color:#fffaf0;"></div>

==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sulfolobus islandicus REY15A]]
[[Category: DuPrez K]]
[[Category: Fan L]]
[[Category: Han X]]
[[Category: Shen Y]]
[[Category: Yuan Z]]
[[Category: Zhai B]]