2R4G

The high resolution structure of the RNA-binding domain of telomerase

Summary for 2R4G

• Entry DOI: 10.2210/pdb2r4g/pdb
• Descriptor: Telomerase reverse transcriptase, BROMIDE ION (3 entities in total)
• Functional Keywords: telomeres, telomerase, chromosomal protein, dna-binding, nucleotidyltransferase, nucleus, rna-directed dna polymerase, transferase
• Biological source: Tetrahymena thermophila
• Cellular location: Nucleus: O77448
• Total number of polymer chains: 1
• Total formula weight: 32992.13

Authors

Rouda, S.,Skordalakes, E. (deposition date: 2007-08-31, release date: 2007-11-13, Last modification date: 2024-02-21)

Primary citation

Rouda, S.,Skordalakes, E.
Structure of the RNA-Binding Domain of Telomerase: Implications for RNA Recognition and Binding.
Structure, 15:1403-1412, 2007

PubMed Abstract: Telomerase, a ribonucleoprotein complex, replicates the linear ends of eukaryotic chromosomes, thus taking care of the "end of replication problem." TERT contains an essential and universally conserved domain (TRBD) that makes extensive contacts with the RNA (TER) component of the holoenzyme, and this interaction is thought to facilitate TERT/TER assembly and repeat-addition processivity. Here, we present a high-resolution structure of TRBD from Tetrahymena thermophila. The nearly all-helical structure comprises a nucleic acid-binding fold suitable for TER binding. An extended pocket on the surface of the protein, formed by two conserved motifs (CP and T motifs) comprises TRBD's RNA-binding pocket. The width and the chemical nature of this pocket suggest that it binds both single- and double-stranded RNA, possibly stem I, and the template boundary element (TBE). Moreover, the structure provides clues into the role of this domain in TERT/TER stabilization and telomerase repeat-addition processivity.

PubMed: 17997966
DOI: 10.1016/j.str.2007.09.007

Experimental method

X-RAY DIFFRACTION (1.71 Å)