8ftm

Setx-ssRNA-ADP-SO4 complex

spinqualitylabelsall models 8ftm, resolution 3.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ftm is a 4 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.01Å Ligands: ADP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0S163_CHATD Publication Abstract from PubMed The senataxin (SETX, Sen1 in yeasts) RNA-DNA hybrid resolving helicase regulates multiple nuclear transactions, including DNA replication, transcription, and DNA repair, but the molecular basis for Sen1 activities is ill defined. Here, Sen1 cryoelectron microscopy (cryo-EM) reconstructions reveal an elongated inchworm-like architecture. Sen1 is composed of an amino terminal helical repeat Sen1 N-terminal (Sen1N) regulatory domain that is flexibly linked to its C-terminal SF1B helicase motor core (Sen1(Hel)) via an intrinsically disordered tether. In an autoinhibited state, the Sen1(Sen1N) domain regulates substrate engagement by promoting occlusion of the RNA substrate-binding cleft. The X-ray structure of an activated Sen1(Hel) engaging single-stranded RNA and ADP-SO(4) shows that the enzyme encircles RNA and implicates a single-nucleotide power stroke in the Sen1 RNA translocation mechanism. Together, our data unveil dynamic protein-protein and protein-RNA interfaces underpinning helicase regulation and inactivation of human SETX activity by RNA-binding-deficient mutants in ataxia with oculomotor apraxia 2 neurodegenerative disease. Sen1 architecture: RNA-DNA hybrid resolution, autoregulation, and insights into SETX inactivation in AOA2.,Appel CD, Bermek O, Dandey VP, Wood M, Viverette E, Williams JG, Bouvette J, Riccio AA, Krahn JM, Borgnia MJ, Williams RS Mol Cell. 2023 Oct 19;83(20):3692-3706.e5. doi: 10.1016/j.molcel.2023.09.024. , Epub 2023 Oct 12. PMID:37832548 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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