1u63

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1u63" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u63, resolution 3.40&Aring;" /> '''THE STRUCTURE OF A R...)
Line 1: Line 1:
-
[[Image:1u63.gif|left|200px]]<br /><applet load="1u63" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1u63.gif|left|200px]]<br /><applet load="1u63" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u63, resolution 3.40&Aring;" />
caption="1u63, resolution 3.40&Aring;" />
'''THE STRUCTURE OF A RIBOSOMAL PROTEIN L1-mRNA COMPLEX'''<br />
'''THE STRUCTURE OF A RIBOSOMAL PROTEIN L1-mRNA COMPLEX'''<br />
==Overview==
==Overview==
-
The RNA-binding ability of ribosomal protein L1 is of profound interest, since the protein has a dual function as a ribosomal protein binding rRNA, and as a translational repressor binding its mRNA. Here, we report the, crystal structure of ribosomal protein L1 in complex with a specific, fragment of its mRNA and compare it with the structure of L1 in complex, with a specific fragment of 23S rRNA determined earlier. In both, complexes, a strongly conserved RNA structural motif is involved in L1, binding through a conserved network of RNA-protein H-bonds inaccessible to, the solvent. These interactions should be responsible for specific, recognition between the protein and RNA. A large number of additional, non-conserved RNA-protein H-bonds stabilizes both complexes. The added, contribution of these non-conserved H-bonds makes the ribosomal complex, much more stable than the regulatory one.
+
The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.
==About this Structure==
==About this Structure==
-
1U63 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U63 OCA].
+
1U63 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U63 OCA].
==Reference==
==Reference==
Line 26: Line 26:
[[Category: ribosome]]
[[Category: ribosome]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:52:24 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:56 2008''

Revision as of 13:20, 21 February 2008


1u63, resolution 3.40Å

Drag the structure with the mouse to rotate

THE STRUCTURE OF A RIBOSOMAL PROTEIN L1-mRNA COMPLEX

Overview

The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA-protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA-protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.

About this Structure

1U63 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA., Nevskaya N, Tishchenko S, Gabdoulkhakov A, Nikonova E, Nikonov O, Nikulin A, Platonova O, Garber M, Nikonov S, Piendl W, Nucleic Acids Res. 2005 Jan 19;33(2):478-85. Print 2005. PMID:15659579

Page seeded by OCA on Thu Feb 21 15:20:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools