2ob7

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(New page: 200px<br /><applet load="2ob7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ob7" /> '''Structure of tmRNA-(SmpB)2 complex as inferr...)
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'''Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM'''<br />
'''Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM'''<br />
==Overview==
==Overview==
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A eubacterial ribosome stalled on a defective mRNA can be released through, a quality control mechanism referred to as trans-translation, which, depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron, microscopy, we obtained a map of the complex composed of a stalled, ribosome and small protein B, which appears near the decoding center. This, result suggests that, when lacking a codon, the A-site on the small, subunit is a target for small protein B. To investigate the role of S1, played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs, but in the absence of S1. In this complex, several connections between the, 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are, no longer found. We propose the unifying concept of scaffolding for the, roles of small protein B and S1 in binding of transfer-messenger RNA to, the ribosome during trans-translation, and we infer a pathway of, sequential binding events in the initial phase of trans-translation.
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A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation.
==About this Structure==
==About this Structure==
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2OB7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OB7 OCA].
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2OB7 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OB7 OCA].
==Reference==
==Reference==
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[[Category: tmrna]]
[[Category: tmrna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:07:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:30 2008''

Revision as of 16:16, 21 February 2008

Image:2ob7.gif

2ob7

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Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM

Overview

A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation.

About this Structure

2OB7 is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1., Gillet R, Kaur S, Li W, Hallier M, Felden B, Frank J, J Biol Chem. 2007 Mar 2;282(9):6356-63. Epub 2006 Dec 19. PMID:17179154

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