7a8r

Structure of RecQL from Bos taurusStructure of RecQL from Bos taurus

Structural highlights 7a8r is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.31Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0JN36_BOVIN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase 3D structures

spinqualitylabelsall models 7a8r, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image