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6D6V

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

Summary for 6D6V
Entry DOI10.2210/pdb6d6v/pdb
EMDB information7820 7821
DescriptorTelomerase reverse transcriptase, Telomerase-associated protein 82, Telomerase holoenzyme TEB heterotrimer Teb3 subunit, ... (9 entities in total)
Functional Keywordstelomerase, telomere, replication
Biological sourceTetrahymena thermophila
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Total number of polymer chains8
Total formula weight394987.00
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 citationJiang, 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: 29775593
DOI: 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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数据于2024-11-06公开中

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