1duh

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(New page: 200px<br /><applet load="1duh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1duh, resolution 2.70&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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caption="1duh, resolution 2.70&Aring;" />
caption="1duh, resolution 2.70&Aring;" />
'''CRYSTAL STRUCTURE OF THE CONSERVED DOMAIN IV OF E. COLI 4.5S RNA'''<br />
'''CRYSTAL STRUCTURE OF THE CONSERVED DOMAIN IV OF E. COLI 4.5S RNA'''<br />
==Overview==
==Overview==
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BACKGROUND: Bacterial signal recognition particle (SRP), consisting of, 4.5S RNA and Ffh protein, plays an essential role in targeting, signal-peptide-containing proteins to the secretory apparatus in the cell, membrane. The 4.5S RNA increases the affinity of Ffh for signal peptides, and is essential for the interaction between SRP and its receptor, protein, FtsY. The 4.5S RNA also interacts with elongation factor G (EF-G) in the, ribosome and this interaction is required for efficient translation., RESULTS: We have determined by multiple anomalous dispersion (MAD) with, Lu(3+) the 2.7 A crystal structure of a 4.5S RNA fragment containing, binding sites for both Ffh and EF-G. This fragment consists of three, helices connected by a symmetric and an asymmetric internal loop. In, contrast to NMR-derived structures reported previously, the symmetric loop, is entirely constituted by non-canonical base pairs. These pairs, continuously stack and project unusual sets of hydrogen-bond donors and, acceptors into the shallow minor groove. The structure can therefore be, regarded as two double helical rods hinged by the asymmetric loop that, protrudes from one strand. CONCLUSIONS: Based on our crystal structure and, results of chemical protection experiments reported previously, we, predicted that Ffh binds to the minor groove of the symmetric loop. An, identical decanucleotide sequence is found in the EF-G binding sites of, both 4.5S RNA and 23S rRNA. The decanucleotide structure in the 4.5S RNA, and the ribosomal protein L11-RNA complex crystals suggests how 4.5S RNA, and 23S rRNA might interact with EF-G and function in translating, ribosomes.
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BACKGROUND: Bacterial signal recognition particle (SRP), consisting of 4.5S RNA and Ffh protein, plays an essential role in targeting signal-peptide-containing proteins to the secretory apparatus in the cell membrane. The 4.5S RNA increases the affinity of Ffh for signal peptides and is essential for the interaction between SRP and its receptor, protein FtsY. The 4.5S RNA also interacts with elongation factor G (EF-G) in the ribosome and this interaction is required for efficient translation. RESULTS: We have determined by multiple anomalous dispersion (MAD) with Lu(3+) the 2.7 A crystal structure of a 4.5S RNA fragment containing binding sites for both Ffh and EF-G. This fragment consists of three helices connected by a symmetric and an asymmetric internal loop. In contrast to NMR-derived structures reported previously, the symmetric loop is entirely constituted by non-canonical base pairs. These pairs continuously stack and project unusual sets of hydrogen-bond donors and acceptors into the shallow minor groove. The structure can therefore be regarded as two double helical rods hinged by the asymmetric loop that protrudes from one strand. CONCLUSIONS: Based on our crystal structure and results of chemical protection experiments reported previously, we predicted that Ffh binds to the minor groove of the symmetric loop. An identical decanucleotide sequence is found in the EF-G binding sites of both 4.5S RNA and 23S rRNA. The decanucleotide structure in the 4.5S RNA and the ribosomal protein L11-RNA complex crystals suggests how 4.5S RNA and 23S rRNA might interact with EF-G and function in translating ribosomes.
==About this Structure==
==About this Structure==
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1DUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with LU, MG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DUH OCA].
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1DUH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=LU:'>LU</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DUH OCA].
==Reference==
==Reference==
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[[Category: Nagai, K.]]
[[Category: Nagai, K.]]
[[Category: Oubridge, C.]]
[[Category: Oubridge, C.]]
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[[Category: Scott, W.G.]]
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[[Category: Scott, W G.]]
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[[Category: Sixma, T.K.]]
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[[Category: Sixma, T K.]]
[[Category: Skarzynski, T.]]
[[Category: Skarzynski, T.]]
[[Category: Wonacott, A.]]
[[Category: Wonacott, A.]]
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[[Category: SO4]]
[[Category: SO4]]
[[Category: 23s rna]]
[[Category: 23s rna]]
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[[Category: 4.5s rna]]
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[[Category: 4 5s rna]]
[[Category: domain iv]]
[[Category: domain iv]]
[[Category: ef-g]]
[[Category: ef-g]]
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[[Category: srp54]]
[[Category: srp54]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:41:47 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:35 2008''

Revision as of 10:20, 21 February 2008

Image:1duh.gif

1duh, resolution 2.70Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE CONSERVED DOMAIN IV OF E. COLI 4.5S RNA

Overview

BACKGROUND: Bacterial signal recognition particle (SRP), consisting of 4.5S RNA and Ffh protein, plays an essential role in targeting signal-peptide-containing proteins to the secretory apparatus in the cell membrane. The 4.5S RNA increases the affinity of Ffh for signal peptides and is essential for the interaction between SRP and its receptor, protein FtsY. The 4.5S RNA also interacts with elongation factor G (EF-G) in the ribosome and this interaction is required for efficient translation. RESULTS: We have determined by multiple anomalous dispersion (MAD) with Lu(3+) the 2.7 A crystal structure of a 4.5S RNA fragment containing binding sites for both Ffh and EF-G. This fragment consists of three helices connected by a symmetric and an asymmetric internal loop. In contrast to NMR-derived structures reported previously, the symmetric loop is entirely constituted by non-canonical base pairs. These pairs continuously stack and project unusual sets of hydrogen-bond donors and acceptors into the shallow minor groove. The structure can therefore be regarded as two double helical rods hinged by the asymmetric loop that protrudes from one strand. CONCLUSIONS: Based on our crystal structure and results of chemical protection experiments reported previously, we predicted that Ffh binds to the minor groove of the symmetric loop. An identical decanucleotide sequence is found in the EF-G binding sites of both 4.5S RNA and 23S rRNA. The decanucleotide structure in the 4.5S RNA and the ribosomal protein L11-RNA complex crystals suggests how 4.5S RNA and 23S rRNA might interact with EF-G and function in translating ribosomes.

About this Structure

1DUH is a Single protein structure of sequence from [1] with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA., Jovine L, Hainzl T, Oubridge C, Scott WG, Li J, Sixma TK, Wonacott A, Skarzynski T, Nagai K, Structure. 2000 May 15;8(5):527-40. PMID:10801497

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