2noq: Difference between revisions

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New page: left|200px<br /><applet load="2noq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2noq" /> '''Structure of ribosome-bound cricket paralysi...
 
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[[Image:2noq.gif|left|200px]]<br /><applet load="2noq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2noq.gif|left|200px]]<br /><applet load="2noq" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2noq" />
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'''Structure of ribosome-bound cricket paralysis virus IRES RNA'''<br />
'''Structure of ribosome-bound cricket paralysis virus IRES RNA'''<br />


==Overview==
==Overview==
Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of, dicistroviral IRESs can assemble elongation-competent 80S ribosomal, complexes in the absence of canonical initiation factors and initiator, transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral, IRES bound to the 80S ribosome. The resolution of the cryo-EM, reconstruction, in the subnanometer range, allowed the molecular structure, of the complete IRES in its active, ribosome-bound state to be solved. The, structure, harboring three pseudoknot-containing domains, each with a, specific functional role, shows how defined elements of the IRES emerge, from a compactly folded core and interact with the key ribosomal, components that form the A, P and E sites, where tRNAs normally bind. Our, results exemplify the molecular strategy for recruitment of an IRES and, reveal the dynamic features necessary for internal initiation.
Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation.


==About this Structure==
==About this Structure==
2NOQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NOQ OCA].  
2NOQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NOQ OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Connell, S.R.]]
[[Category: Connell, S R.]]
[[Category: Dabrowski, M.]]
[[Category: Dabrowski, M.]]
[[Category: Giesebrecht, J.]]
[[Category: Giesebrecht, J.]]
[[Category: Lescoute, A.]]
[[Category: Lescoute, A.]]
[[Category: Mielke, T.]]
[[Category: Mielke, T.]]
[[Category: Penczek, P.A.]]
[[Category: Penczek, P A.]]
[[Category: Schroeer, B.]]
[[Category: Schroeer, B.]]
[[Category: Schuler, M.]]
[[Category: Schuler, M.]]
[[Category: Spahn, C.M.T.]]
[[Category: Spahn, C M.T.]]
[[Category: Westhof, E.]]
[[Category: Westhof, E.]]
[[Category: internal initiation]]
[[Category: internal initiation]]
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[[Category: translation]]
[[Category: translation]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:49:05 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:11 2008''

Revision as of 19:09, 21 February 2008

File:2noq.gif


2noq

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Structure of ribosome-bound cricket paralysis virus IRES RNA

OverviewOverview

Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initiation factors and initiator transfer RNA. We present here a cryo-EM reconstruction of a dicistroviral IRES bound to the 80S ribosome. The resolution of the cryo-EM reconstruction, in the subnanometer range, allowed the molecular structure of the complete IRES in its active, ribosome-bound state to be solved. The structure, harboring three pseudoknot-containing domains, each with a specific functional role, shows how defined elements of the IRES emerge from a compactly folded core and interact with the key ribosomal components that form the A, P and E sites, where tRNAs normally bind. Our results exemplify the molecular strategy for recruitment of an IRES and reveal the dynamic features necessary for internal initiation.

About this StructureAbout this Structure

2NOQ is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the ribosome-bound cricket paralysis virus IRES RNA., Schuler M, Connell SR, Lescoute A, Giesebrecht J, Dabrowski M, Schroeer B, Mielke T, Penczek PA, Westhof E, Spahn CM, Nat Struct Mol Biol. 2006 Dec;13(12):1092-6. Epub 2006 Nov 19. PMID:17115051

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