2r4g
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(New page: 200px<br /><applet load="2r4g" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r4g, resolution 1.71Å" /> '''The high resolution ...)
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Revision as of 10:06, 23 January 2008
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The high resolution structure of the RNA-binding domain of telomerase
Overview
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.
About this Structure
2R4G is a Single protein structure of sequence from Tetrahymena thermophila with as ligand. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.
Reference
Structure of the RNA-Binding Domain of Telomerase: Implications for RNA Recognition and Binding., Rouda S, Skordalakes E, Structure. 2007 Nov 13;15(11):1403-1412. PMID:17997966
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