4eyt

Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65

spinqualitylabelsall models 4eyt, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4eyt is a 6 chain structure with sequence from Tetrahymena thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LARP7_TETTS RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:15131081, PubMed:15696174, PubMed:16507983, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372). Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:15696174, PubMed:17322903, PubMed:20713447). TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain (PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372). See Also Telomerase-associated protein

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