7a8r: Difference between revisions
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==Structure of RecQL from Bos taurus== | |||
<StructureSection load='7a8r' size='340' side='right'caption='[[7a8r]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7a8r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7A8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A8R 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]] 2.31Å</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=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=7a8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a8r OCA], [https://pdbe.org/7a8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a8r RCSB], [https://www.ebi.ac.uk/pdbsum/7a8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a8r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0JN36_BOVIN A0JN36_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
There is broad consensus that RecQ family helicase is a high-order oligomer that dissociates into a dimer upon ATP binding. This conclusion is based mainly on studies of highly purified recombinant proteins, and the oligomeric states of RecQ helicases in living cells remain unknown. We show here that, in contrast to current models, monomeric RECQL helicase is more abundant than oligomer/dimer forms in living cells. Further characterization of endogenous BtRECQL and isolated monomeric BtRECQL using various approaches demonstrates that both endogenous and recombinant monomeric BtRECQL effectively function as monomers, displaying higher helicase and ATPase activities than dimers and oligomers. Furthermore, monomeric BtRECQL unfolds intramolecular G-quadruplex DNA as efficiently as human RECQL and BLM helicases. These discoveries have implications for understanding endogenous RECQL oligomeric structures and their regulation. It is worth revisiting oligomeric states of the other members of the RecQ family helicases in living cells. | |||
Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers.,Liu NN, Song ZY, Guo HL, Yin H, Chen WF, Dai YX, Xin BG, Ai X, Ji L, Wang QM, Hou XM, Dou SX, Rety S, Xi XG Cell Rep. 2021 Sep 7;36(10):109688. doi: 10.1016/j.celrep.2021.109688. PMID:34496242<ref>PMID:34496242</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7a8r" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen WF]] | |||
[[Category: Rety S]] | |||
[[Category: Xi XG]] | |||
Latest revision as of 15:05, 1 February 2024
Structure of RecQL from Bos taurusStructure of RecQL from Bos taurus
Structural highlights
FunctionPublication Abstract from PubMedThere is broad consensus that RecQ family helicase is a high-order oligomer that dissociates into a dimer upon ATP binding. This conclusion is based mainly on studies of highly purified recombinant proteins, and the oligomeric states of RecQ helicases in living cells remain unknown. We show here that, in contrast to current models, monomeric RECQL helicase is more abundant than oligomer/dimer forms in living cells. Further characterization of endogenous BtRECQL and isolated monomeric BtRECQL using various approaches demonstrates that both endogenous and recombinant monomeric BtRECQL effectively function as monomers, displaying higher helicase and ATPase activities than dimers and oligomers. Furthermore, monomeric BtRECQL unfolds intramolecular G-quadruplex DNA as efficiently as human RECQL and BLM helicases. These discoveries have implications for understanding endogenous RECQL oligomeric structures and their regulation. It is worth revisiting oligomeric states of the other members of the RecQ family helicases in living cells. Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers.,Liu NN, Song ZY, Guo HL, Yin H, Chen WF, Dai YX, Xin BG, Ai X, Ji L, Wang QM, Hou XM, Dou SX, Rety S, Xi XG Cell Rep. 2021 Sep 7;36(10):109688. doi: 10.1016/j.celrep.2021.109688. PMID:34496242[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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