4LMO

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

4LMO の概要

• エントリーDOI: 10.2210/pdb4lmo/pdb
• 関連するPDBエントリー: 2R4G 3DU5 3DU6
• 分子名称: Telomerase reverse transcriptase (2 entities in total)
• 機能のキーワード: rna binding domain of the reverse transcriptase telomerase, rna binding protein
• 由来する生物種: Takifugu rubripes (tiger puffer)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119024.02

構造登録者

Harkisheimer, M.,Mason, M.,Shuvaeva, E.,Skordalakes, E. (登録日: 2013-07-10, 公開日: 2013-10-09, 最終更新日: 2013-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.37 Å)