1kuq: Difference between revisions

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New page: left|200px<br /><applet load="1kuq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kuq, resolution 2.84Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1kuq.gif|left|200px]]<br /><applet load="1kuq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kuq.gif|left|200px]]<br /><applet load="1kuq" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kuq, resolution 2.84&Aring;" />
caption="1kuq, resolution 2.84&Aring;" />
'''CRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNA'''<br />
'''CRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNA'''<br />


==Overview==
==Overview==
The position and conformation of the N-terminal helix of free ribosomal, protein S15 was earlier found to be modified under various conditions., This variability was supposed to provide the recognition by the protein of, its specific site on 16S rRNA. To test this hypothesis, we substituted, some amino acid residues in this helix and assessed effects of these, substitutions on the affinity of the protein for 16S rRNA. The crystal, structure of the complex of one of these mutants (Thr3Cys S15) with the, 16S rRNA fragment was determined, and a computer model of the complex, containing another mutant (Gln8Met S15) was designed. The available and, new information was analyzed in detail, and the N-terminal helix was, concluded to play no significant role in the specific binding of the S15, protein to its target on 16S rRNA.
The position and conformation of the N-terminal helix of free ribosomal protein S15 was earlier found to be modified under various conditions. This variability was supposed to provide the recognition by the protein of its specific site on 16S rRNA. To test this hypothesis, we substituted some amino acid residues in this helix and assessed effects of these substitutions on the affinity of the protein for 16S rRNA. The crystal structure of the complex of one of these mutants (Thr3Cys S15) with the 16S rRNA fragment was determined, and a computer model of the complex containing another mutant (Gln8Met S15) was designed. The available and new information was analyzed in detail, and the N-terminal helix was concluded to play no significant role in the specific binding of the S15 protein to its target on 16S rRNA.


==About this Structure==
==About this Structure==
1KUQ 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KUQ OCA].  
1KUQ 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUQ OCA].  


==Reference==
==Reference==
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[[Category: Nevskaya, N.]]
[[Category: Nevskaya, N.]]
[[Category: Nikonov, S.]]
[[Category: Nikonov, S.]]
[[Category: Nikulin, A.D.]]
[[Category: Nikulin, A D.]]
[[Category: Revtovich, S.]]
[[Category: Revtovich, S.]]
[[Category: Tishchenko, S.]]
[[Category: Tishchenko, S.]]
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[[Category: rrna-protein complex]]
[[Category: rrna-protein complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:53:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:05 2008''

Revision as of 14:38, 21 February 2008

File:1kuq.gif


1kuq, resolution 2.84Å

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CRYSTAL STRUCTURE OF T3C MUTANT S15 RIBOSOMAL PROTEIN IN COMPLEX WITH 16S RRNA

OverviewOverview

The position and conformation of the N-terminal helix of free ribosomal protein S15 was earlier found to be modified under various conditions. This variability was supposed to provide the recognition by the protein of its specific site on 16S rRNA. To test this hypothesis, we substituted some amino acid residues in this helix and assessed effects of these substitutions on the affinity of the protein for 16S rRNA. The crystal structure of the complex of one of these mutants (Thr3Cys S15) with the 16S rRNA fragment was determined, and a computer model of the complex containing another mutant (Gln8Met S15) was designed. The available and new information was analyzed in detail, and the N-terminal helix was concluded to play no significant role in the specific binding of the S15 protein to its target on 16S rRNA.

About this StructureAbout this Structure

1KUQ is a Single protein structure of sequence from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Role of N-terminal helix in interaction of ribosomal protein S15 with 16S rRNA., Revtovich SV, Nikulin AD, Nikonov SV, Biochemistry (Mosc). 2004 Dec;69(12):1319-23. PMID:15627386

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