5DFM

Structure of Tetrahymena telomerase p19 fused to MBP

Summary for 5DFM

• Entry DOI: 10.2210/pdb5dfm/pdb
• Related: 5DFN
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein,Telomerase-associated protein 19, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (5 entities in total)
• Functional Keywords: telomerase, p19, cst complex, ten1, ob-fold, oligonucleotide binding fold, nuclear protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 122016.92

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 citation

Jiang, 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

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

Experimental method

X-RAY DIFFRACTION (2.301 Å)