7A8R
Structure of RecQL from Bos taurus
Summary for 7A8R
Entry DOI | 10.2210/pdb7a8r/pdb |
Descriptor | ATP-dependent DNA helicase, ZINC ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
Functional Keywords | helicase, dna repair, holliday junction, recombination |
Biological source | Bos taurus (Bovine) |
Total number of polymer chains | 2 |
Total formula weight | 122144.49 |
Authors | Rety, S.,Chen, W.F.,Xi, X.G. (deposition date: 2020-08-30, release date: 2021-10-06, Last modification date: 2024-01-31) |
Primary citation | Liu, N.N.,Song, Z.Y.,Guo, H.L.,Yin, H.,Chen, W.F.,Dai, Y.X.,Xin, B.G.,Ai, X.,Ji, L.,Wang, Q.M.,Hou, X.M.,Dou, S.X.,Rety, S.,Xi, X.G. Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers. Cell Rep, 36:109688-109688, 2021 Cited by PubMed Abstract: 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. PubMed: 34496242DOI: 10.1016/j.celrep.2021.109688 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
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