1p6v

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(New page: 200px<br /><applet load="1p6v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p6v, resolution 3.20&Aring;" /> '''Crystal structure of...)
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[[Image:1p6v.gif|left|200px]]<br /><applet load="1p6v" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p6v, resolution 3.20&Aring;" />
caption="1p6v, resolution 3.20&Aring;" />
'''Crystal structure of the tRNA domain of transfer-messenger RNA in complex with SmpB'''<br />
'''Crystal structure of the tRNA domain of transfer-messenger RNA in complex with SmpB'''<br />
==Overview==
==Overview==
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Accurate translation of genetic information into protein sequence depends, on complete messenger RNA molecules. Truncated mRNAs cause synthesis of, defective proteins, and arrest ribosomes at the end of their incomplete, message. In bacteria, a hybrid RNA molecule that combines the functions of, both transfer and messenger RNAs (called tmRNA) rescues stalled ribosomes, and targets aberrant, partially synthesized, proteins for proteolytic, degradation. Here we report the 3.2-A-resolution structure of the, tRNA-like domain of tmRNA (tmRNA(Delta)) in complex with small protein B, (SmpB), a protein essential for biological functions of tmRNA. We find, that the flexible RNA molecule adopts an open L-shaped conformation and, SmpB binds to its elbow region, stabilizing the single-stranded D-loop in, an extended conformation. The most striking feature of the structure of, tmRNA(Delta) is a 90 degrees rotation of the TPsiC-arm around the helical, axis. Owing to this unusual conformation, the SmpB-tmRNA(Delta) complex, positioned into the A-site of the ribosome orients SmpB towards the small, ribosomal subunit, and directs tmRNA towards the elongation-factor binding, region of the ribosome. On the basis of this structure, we propose a model, for the binding of tmRNA on the ribosome.
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Accurate translation of genetic information into protein sequence depends on complete messenger RNA molecules. Truncated mRNAs cause synthesis of defective proteins, and arrest ribosomes at the end of their incomplete message. In bacteria, a hybrid RNA molecule that combines the functions of both transfer and messenger RNAs (called tmRNA) rescues stalled ribosomes, and targets aberrant, partially synthesized, proteins for proteolytic degradation. Here we report the 3.2-A-resolution structure of the tRNA-like domain of tmRNA (tmRNA(Delta)) in complex with small protein B (SmpB), a protein essential for biological functions of tmRNA. We find that the flexible RNA molecule adopts an open L-shaped conformation and SmpB binds to its elbow region, stabilizing the single-stranded D-loop in an extended conformation. The most striking feature of the structure of tmRNA(Delta) is a 90 degrees rotation of the TPsiC-arm around the helical axis. Owing to this unusual conformation, the SmpB-tmRNA(Delta) complex positioned into the A-site of the ribosome orients SmpB towards the small ribosomal subunit, and directs tmRNA towards the elongation-factor binding region of the ribosome. On the basis of this structure, we propose a model for the binding of tmRNA on the ribosome.
==About this Structure==
==About this Structure==
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1P6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P6V OCA].
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1P6V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6V OCA].
==Reference==
==Reference==
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[[Category: Felden, B.]]
[[Category: Felden, B.]]
[[Category: Gutmann, S.]]
[[Category: Gutmann, S.]]
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[[Category: Haebel, P.W.]]
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[[Category: Haebel, P W.]]
[[Category: Metzinger, L.]]
[[Category: Metzinger, L.]]
[[Category: Sutter, M.]]
[[Category: Sutter, M.]]
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[[Category: trans-translation]]
[[Category: trans-translation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:31:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:45 2008''

Revision as of 12:25, 21 February 2008


1p6v, resolution 3.20Å

Drag the structure with the mouse to rotate

Crystal structure of the tRNA domain of transfer-messenger RNA in complex with SmpB

Overview

Accurate translation of genetic information into protein sequence depends on complete messenger RNA molecules. Truncated mRNAs cause synthesis of defective proteins, and arrest ribosomes at the end of their incomplete message. In bacteria, a hybrid RNA molecule that combines the functions of both transfer and messenger RNAs (called tmRNA) rescues stalled ribosomes, and targets aberrant, partially synthesized, proteins for proteolytic degradation. Here we report the 3.2-A-resolution structure of the tRNA-like domain of tmRNA (tmRNA(Delta)) in complex with small protein B (SmpB), a protein essential for biological functions of tmRNA. We find that the flexible RNA molecule adopts an open L-shaped conformation and SmpB binds to its elbow region, stabilizing the single-stranded D-loop in an extended conformation. The most striking feature of the structure of tmRNA(Delta) is a 90 degrees rotation of the TPsiC-arm around the helical axis. Owing to this unusual conformation, the SmpB-tmRNA(Delta) complex positioned into the A-site of the ribosome orients SmpB towards the small ribosomal subunit, and directs tmRNA towards the elongation-factor binding region of the ribosome. On the basis of this structure, we propose a model for the binding of tmRNA on the ribosome.

About this Structure

1P6V is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB., Gutmann S, Haebel PW, Metzinger L, Sutter M, Felden B, Ban N, Nature. 2003 Aug 7;424(6949):699-703. PMID:12904796

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