2r4g
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Telomerase, a ribonucleoprotein complex, replicates the linear ends of | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structure of the RNA- | + | Structure of the RNA-binding domain of telomerase: implications for RNA recognition and binding., Rouda S, Skordalakes E, Structure. 2007 Nov;15(11):1403-12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17997966 17997966] |
[[Category: RNA-directed DNA polymerase]] | [[Category: RNA-directed DNA polymerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:44:32 2008'' |
Revision as of 16:44, 21 February 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;15(11):1403-12. PMID:17997966
Page seeded by OCA on Thu Feb 21 18:44:32 2008
