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5DFN

Structure of Tetrahymena Telomerase P45 C-terminal domain

Summary for 5DFN
Entry DOI10.2210/pdb5dfn/pdb
Related5DFM
DescriptorTelomerase associated protein p45 (2 entities in total)
Functional Keywordstelomerase, p45, cst complex, stn1, winged helix, wh domain, whth, winged helix turn helix, nuclear protein
Biological sourceTetrahymena thermophila
Total number of polymer chains2
Total formula weight50421.33
Authors
Chan, H.,Cascio, D.,Sawaya, M.R.,Feigon, J. (deposition date: 2015-08-27, release date: 2015-10-28, Last modification date: 2024-03-06)
Primary citationJiang, J.,Chan, H.,Cash, D.D.,Miracco, E.J.,Ogorzalek Loo, R.R.,Upton, H.E.,Cascio, D.,O'Brien Johnson, R.,Collins, K.,Loo, J.A.,Zhou, Z.H.,Feigon, J.
Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.
Science, 350:aab4070-aab4070, 2015
Cited by
PubMed Abstract: Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function.
PubMed: 26472759
DOI: 10.1126/science.aab4070
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.382 Å)
Structure validation

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