View source for 5lb5


==Crystal structure of human RECQL5 helicase in complex with ADP/Mg (tricilinc form).==
<StructureSection load='5lb5' size='340' side='right'caption='[[5lb5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lb5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LB5 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5lb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lb5 OCA], [https://pdbe.org/5lb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lb5 RCSB], [https://www.ebi.ac.uk/pdbsum/5lb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lb5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECQ5_HUMAN RECQ5_HUMAN] May have an important role in DNA metabolism.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RecQ helicases are important maintainers of genome integrity with distinct roles in almost every cellular process requiring access to DNA. RECQL5 is one of five human RecQ proteins and is particularly versatile in this regard, forming protein complexes with a diverse set of cellular partners in order to coordinate its helicase activity to various processes including replication, recombination and DNA repair. In this study, we have determined crystal structures of the core helicase domain of RECQL5 both with and without the nucleotide ADP in two distinctly different ('Open' and 'Closed') conformations. Small angle X-ray scattering studies show that the 'Open' form of the protein predominates in solution and we discuss implications of this with regards to the RECQL5 mechanism and conformational changes. We have measured the ATPase, helicase and DNA binding properties of various RECQL5 constructs and variants and discuss the role of these regions and residues in the various RECQL5 activities. Finally, we have performed a systematic comparison of the RECQL5 structures with other RecQ family structures and based on these comparisons we have constructed a model for the mechano-chemical cycle of the common catalytic core of these helicases.

Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.,Newman JA, Aitkenhead H, Savitsky P, Gileadi O Nucleic Acids Res. 2017 Jan 18. pii: gkw1362. doi: 10.1093/nar/gkw1362. PMID:28100692<ref>PMID:28100692</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lb5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aitkenhead H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Edwards AM]]
[[Category: Gileadi O]]
[[Category: Krojer T]]
[[Category: Newman JA]]
[[Category: Savitsky P]]
[[Category: Von Delft F]]