PDBsum entry 4lmo

RNA binding protein

PDB id: 4lmo

Contents

Protein chains

251 a.a.

Waters ×144

PDB id:

4lmo

Name:

RNA binding protein

Title:

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

Structure:

Telomerase reverse transcriptase. Chain: a, b, c, d. Fragment: RNA binding domain (unp residues 295-544). Engineered: yes

Source:

Takifugu rubripes. Tiger puffer. Organism_taxid: 31033. Gene: tert. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.37Å R-factor: 0.222 R-free: 0.259

Authors:

M.Harkisheimer,M.Mason,E.Shuvaeva,E.Skordalakes

Key ref:

M.Harkisheimer et al. (2013). A motif in the vertebrate telomerase N-terminal linker of TERT contributes to RNA binding and telomerase activity and processivity. Structure, 21, 1870-1878. PubMed id: 24055314 DOI: 10.1016/j.str.2013.08.013

Date:

10-Jul-13 Release date: 09-Oct-13

Protein chains

Q4KTA7  (TERT_TAKRU) -  Telomerase reverse transcriptase from Takifugu rubripes

Seq: 1074 a.a.

Struc: 251 a.a.

Enzyme reactions

• Enzyme class: E.C.2.7.7.49 - RNA-directed Dna polymerase.
• Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.str.2013.08.013

Structure 21:1870-1878 (2013)

PubMed id: 24055314

A motif in the vertebrate telomerase N-terminal linker of TERT contributes to RNA binding and telomerase activity and processivity.

M.Harkisheimer, M.Mason, E.Shuvaeva, E.Skordalakes.

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.