1zho
From Proteopedia
(New page: 200px<br /><applet load="1zho" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zho, resolution 2.60Å" /> '''The structure of a r...) |
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| - | [[Image:1zho.gif|left|200px]]<br /><applet load="1zho" size=" | + | [[Image:1zho.gif|left|200px]]<br /><applet load="1zho" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zho, resolution 2.60Å" /> | caption="1zho, resolution 2.60Å" /> | ||
'''The structure of a ribosomal protein L1 in complex with mRNA'''<br /> | '''The structure of a ribosomal protein L1 in complex with mRNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds | + | The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1ZHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZHO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna-protein interaction]] | [[Category: rna-protein interaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:15:36 2008'' |
Revision as of 14:15, 21 February 2008
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The structure of a ribosomal protein L1 in complex with mRNA
Overview
The RNA-binding ability of ribosomal protein L1 is of profound interest, since L1 has a dual function as a ribosomal structural protein that binds rRNA and as a translational repressor that binds its own mRNA. Here, we report the crystal structure at 2.6 A resolution of ribosomal protein L1 from the bacterium Thermus thermophilus in complex with a 38 nt fragment of L1 mRNA from Methanoccocus vannielii. The conformation of RNA-bound T.thermophilus L1 differs dramatically from that of the isolated protein. Analysis of four copies of the L1-mRNA complex in the crystal has shown that domain II of the protein does not contribute to mRNA-specific binding. A detailed comparison of the protein-RNA interactions in the L1-mRNA and L1-rRNA complexes identified amino acid residues of L1 crucial for recognition of its specific targets on the both RNAs. Incorporation of the structure of bacterial L1 into a model of the Escherichia coli ribosome revealed two additional contact regions for L1 on the 23S rRNA that were not identified in previous ribosome models.
About this Structure
1ZHO is a Single protein structure of sequence from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.
Reference
New insights into the interaction of ribosomal protein L1 with RNA., Nevskaya N, Tishchenko S, Volchkov S, Kljashtorny V, Nikonova E, Nikonov O, Nikulin A, Kohrer C, Piendl W, Zimmermann R, Stockley P, Garber M, Nikonov S, J Mol Biol. 2006 Jan 27;355(4):747-59. Epub 2005 Nov 17. PMID:16330048
Page seeded by OCA on Thu Feb 21 16:15:36 2008
Categories: Single protein | Thermus thermophilus | Garber, M. | Kljashtorny, V. | Kohrer, C. | Nevskaya, N. | Nikonov, O. | Nikonov, S. | Nikonova, E. | Nikulin, A. | Piendl, W. | Stockley, P. | Tishchenko, S. | Volchkov, S. | Zimmermann, R. | K | L1 | Mrna-protein complex | Regulation of gene expression | Ribosomal protein | Ribosome | Rna-protein interaction
