4ERD

Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65 in complex with stem IV of telomerase RNA

Summary for 4ERD

• Entry DOI: 10.2210/pdb4erd/pdb
• Related: 4EYT
• Descriptor: Telomerase associated protein p65, 5'-R(P*GP*GP*UP*CP*GP*AP*CP*AP*UP*CP*UP*UP*CP*GP*GP*AP*UP*GP*GP*AP*CP*C)-3', POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: la protein, larp7, rrm, xrrm, ter, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 4
• Total formula weight: 45710.96

Authors

Singh, M.,Wang, Z.,Koo, B.-K.,Patel, A.,Cascio, D.,Collins, K.,Feigon, J. (deposition date: 2012-04-19, release date: 2012-06-20, Last modification date: 2024-11-06)

Primary citation

Singh, M.,Wang, Z.,Koo, B.K.,Patel, A.,Cascio, D.,Collins, K.,Feigon, J.
Structural Basis for Telomerase RNA Recognition and RNP Assembly by the Holoenzyme La Family Protein p65.
Mol.Cell, 47:16-26, 2012

PubMed Abstract: Telomerase is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. The catalytic core of Tetrahymena telomerase comprises a ternary complex of telomerase RNA (TER), telomerase reverse transcriptase (TERT), and the essential La family protein p65. NMR and crystal structures of p65 C-terminal domain and its complex with stem IV of TER reveal that RNA recognition is achieved by a combination of single- and double-stranded RNA binding, which induces a 105° bend in TER. The domain is a cryptic, atypical RNA recognition motif with a disordered C-terminal extension that forms an α helix in the complex necessary for hierarchical assembly of TERT with p65-TER. This work provides the first structural insight into biogenesis and assembly of TER with a telomerase-specific protein. Additionally, our studies define a structurally homologous domain (xRRM) in genuine La and LARP7 proteins and suggest a general mode of RNA binding for biogenesis of their diverse RNA targets.

PubMed: 22705372
DOI: 10.1016/j.molcel.2012.05.018

Experimental method

X-RAY DIFFRACTION (2.589 Å)