6D6V
CryoEM structure of Tetrahymena telomerase with telomeric DNA at 4.8 Angstrom resolution
Summary for 6D6V
Entry DOI | 10.2210/pdb6d6v/pdb |
EMDB information | 7820 7821 |
Descriptor | Telomerase reverse transcriptase, Telomerase-associated protein 82, Telomerase holoenzyme TEB heterotrimer Teb3 subunit, ... (9 entities in total) |
Functional Keywords | telomerase, telomere, replication |
Biological source | Tetrahymena thermophila More |
Total number of polymer chains | 8 |
Total formula weight | 394987.00 |
Authors | Jiang, J.,Wang, Y.,Susac, L.,Chan, H.,Basu, R.,Zhou, Z.H.,Feigon, J. (deposition date: 2018-04-22, release date: 2018-05-30, Last modification date: 2024-03-13) |
Primary citation | Jiang, J.,Wang, Y.,Susac, L.,Chan, H.,Basu, R.,Zhou, Z.H.,Feigon, J. Structure of Telomerase with Telomeric DNA. Cell, 173:1179-1190.e13, 2018 Cited by PubMed Abstract: 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 Å 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. PubMed: 29775593DOI: 10.1016/j.cell.2018.04.038 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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