5m89

Spliceosome component

spinqualitylabelsall models 5m89, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m89 is a 2 chain structure with sequence from Chaetomium thermophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.605Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G0SFY0_CHATD Publication Abstract from PubMed Human nineteen complex (NTC) acts as a multimeric E3 ubiquitin ligase in DNA repair and splicing. The transfer of ubiquitin is mediated by Prp19-a homotetrameric component of NTC whose elongated coiled coils serve as an assembly axis for two other proteins called SPF27 and CDC5L. We find that Prp19 is inactive on its own and have elucidated the structural basis of its autoinhibition by crystallography and mutational analysis. Formation of the NTC core by stepwise assembly of SPF27, CDC5L, and PLRG1 onto the Prp19 tetramer enables ubiquitin ligation. Protein-protein crosslinking of NTC, functional assays in vitro, and assessment of its role in DNA damage response provide mechanistic insight into the organization of the NTC core and the communication between PLRG1 and Prp19 that enables E3 activity. This reveals a unique mode of regulation for a complex E3 ligase and advances understanding of its dynamics in various cellular pathways. Prp19/Pso4 Is an Autoinhibited Ubiquitin Ligase Activated by Stepwise Assembly of Three Splicing Factors.,de Moura TR, Mozaffari-Jovin S, Szabo CZK, Schmitzova J, Dybkov O, Cretu C, Kachala M, Svergun D, Urlaub H, Luhrmann R, Pena V Mol Cell. 2018 Mar 15;69(6):979-992.e6. doi: 10.1016/j.molcel.2018.02.022. PMID:29547724 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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