2ob7: Difference between revisions
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[[Image:2ob7.gif|left|200px]] | [[Image:2ob7.gif|left|200px]] | ||
'''Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM''' | {{Structure | ||
|PDB= 2ob7 |SIZE=350|CAPTION= <scene name='initialview01'>2ob7</scene> | |||
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|LIGAND= | |||
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'''Structure of tmRNA-(SmpB)2 complex as inferred from cryo-EM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OB7 is a [ | 2OB7 is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17179154 17179154] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: tmrna]] | [[Category: tmrna]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:57:25 2008'' | ||
Revision as of 15:57, 20 March 2008
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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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