8sok

Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA

spinqualitylabelsall models 8sok, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8sok is a 6 chain structure with sequence from Enterovirus A71, Escherichia coli O157:H7, Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.1Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Telomere maintenance requires the extension of the G-rich telomeric repeat strand by telomerase and the fill-in synthesis of the C-rich strand by Polalpha/primase. At telomeres, Polalpha/primase is bound to Ctc1/Stn1/Ten1 (CST), a single-stranded DNA-binding complex. Like mutations in telomerase, mutations affecting CST-Polalpha/primase result in pathological telomere shortening and cause a telomere biology disorder, Coats plus (CP). We determined cryogenic electron microscopy structures of human CST bound to the shelterin heterodimer POT1/TPP1 that reveal how CST is recruited to telomeres by POT1. Our findings suggest that POT1 hinge phosphorylation is required for CST recruitment, and the complex is formed through conserved interactions involving several residues mutated in CP. Our structural and biochemical data suggest that phosphorylated POT1 holds CST-Polalpha/primase in an inactive, autoinhibited state until telomerase has extended the telomere ends. We propose that dephosphorylation of POT1 releases CST-Polalpha/primase into an active state that completes telomere replication through fill-in synthesis. POT1 recruits and regulates CST-Polalpha/primase at human telomeres.,Cai SW, Takai H, Zaug AJ, Dilgen TC, Cech TR, Walz T, de Lange T Cell. 2024 Jul 11;187(14):3638-3651.e18. doi: 10.1016/j.cell.2024.05.002. Epub , 2024 Jun 4. PMID:38838667 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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