6d6v

CryoEM structure of Tetrahymena telomerase with telomeric DNA at 4.8 Angstrom resolution

Loading... Status: waiting for Mol* initialization Structural highlights 6d6v is a 8 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: Electron Microscopy, Resolution 4.8Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TERT_TETTS Catalytic component of telomerase, 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:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:16462747, PubMed:17322903, PubMed:20713447). Publication Abstract from PubMed Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA (TER). Its activity is a critical determinant of human health, affecting aging, cancer, and stem cell renewal. Lack of atomic models of telomerase, particularly one with DNA bound, has limited our mechanistic understanding of telomeric DNA repeat synthesis. We report the 4.8 A resolution cryoelectron microscopy structure of active Tetrahymena telomerase bound to telomeric DNA. The catalytic core is an intricately interlocked structure of TERT and TER, including a previously structurally uncharacterized TERT domain that interacts with the TEN domain to physically enclose TER and regulate activity. This complete structure of a telomerase catalytic core and its interactions with telomeric DNA from the template to telomere-interacting p50-TEB complex provides unanticipated insights into telomerase assembly and catalytic cycle and a new paradigm for a reverse transcriptase RNP. Structure of Telomerase with Telomeric DNA.,Jiang J, Wang Y, Susac L, Chan H, Basu R, Zhou ZH, Feigon J Cell. 2018 May 17;173(5):1179-1190.e13. doi: 10.1016/j.cell.2018.04.038. PMID:29775593 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Telomerase 3D structures Telomerase-associated protein

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