4O26

Crystal structure of the TRBD domain of TERT and the CR4/5 of TR

Summary for 4O26

• Entry DOI: 10.2210/pdb4o26/pdb
• Descriptor: Telomerase reverse transcriptase, Telomerase TR, SULFATE ION, ... (4 entities in total)
• Functional Keywords: telomerase, telomerase rna, protein-rna interaction, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Oryzias latipes (Japanese rice fish); More
• Total number of polymer chains: 4
• Total formula weight: 93844.35

Authors

Huang, J.,Wu, J.,Lei, M. (deposition date: 2013-12-16, release date: 2014-05-07, Last modification date: 2024-10-30)

Primary citation

Huang, J.,Brown, A.F.,Wu, J.,Xue, J.,Bley, C.J.,Rand, D.P.,Wu, L.,Zhang, R.,Chen, J.J.,Lei, M.
Structural basis for protein-RNA recognition in telomerase.
Nat.Struct.Mol.Biol., 21:507-512, 2014

PubMed Abstract: Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR.

PubMed: 24793650
DOI: 10.1038/nsmb.2819

Experimental method

X-RAY DIFFRACTION (3.001 Å)