4LMO

Structure of a vertebrate RNA binding domain of telomerase (TRBD)

Summary for 4LMO

• Entry DOI: 10.2210/pdb4lmo/pdb
• Related: 2R4G 3DU5 3DU6
• Descriptor: Telomerase reverse transcriptase (2 entities in total)
• Functional Keywords: rna binding domain of the reverse transcriptase telomerase, rna binding protein
• Biological source: Takifugu rubripes (tiger puffer)
• Total number of polymer chains: 4
• Total formula weight: 119024.02

Authors

Harkisheimer, M.,Mason, M.,Shuvaeva, E.,Skordalakes, E. (deposition date: 2013-07-10, release date: 2013-10-09, Last modification date: 2024-11-20)

Primary citation

Harkisheimer, M.,Mason, M.,Shuvaeva, E.,Skordalakes, E.
A Motif in the Vertebrate Telomerase N-Terminal Linker of TERT Contributes to RNA Binding and Telomerase Activity and Processivity.
Structure, 21:1870-1878, 2013

PubMed Abstract: Telomerase is a ribonucleoprotein reverse transcriptase that replicates the ends of chromosomes, thus maintaining genome stability. Telomerase ribonucleoprotein assembly is primarily mediated by the RNA binding domain (TRBD) of the enzyme. Here we present the high-resolution TRBD structure of the vertebrate, Takifugu rubripes (trTRBD). The structure shows that with the exception of the N-terminal linker, the trTRBD is conserved with the Tribolium castaneum and Tetrahymena thermophila TRBDs, suggesting evolutionary conservation across species. The structure provides a view of the structural organization of the vertebrate-specific VSR motif that binds the activation domain (CR4/5) of the RNA component of telomerase. It also reveals a motif (TFLY) that forms part of the T-CP pocket implicated in template boundary element (TBE) binding. Mutant proteins of conserved residues that consist of part of the T and TFLY motifs disrupt trTRBD-TBE binding and telomerase activity and processivity, supporting an essential role of these motifs in telomerase RNP assembly and function.

PubMed: 24055314
DOI: 10.1016/j.str.2013.08.013

Experimental method

X-RAY DIFFRACTION (2.37 Å)