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PDBsum entry 4lmo
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RNA binding protein
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PDB id
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4lmo
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References listed in PDB file
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Key reference
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Title
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A motif in the vertebrate telomerase n-Terminal linker of tert contributes to RNA binding and telomerase activity and processivity.
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Authors
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M.Harkisheimer,
M.Mason,
E.Shuvaeva,
E.Skordalakes.
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Ref.
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Structure, 2013,
21,
1870-1878.
[DOI no: ]
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PubMed id
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Abstract
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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.
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