1rip: Difference between revisions

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New page: left|200px<br /><applet load="1rip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rip" /> '''RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF T...
 
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[[Image:1rip.gif|left|200px]]<br /><applet load="1rip" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rip.gif|left|200px]]<br /><applet load="1rip" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rip" />
caption="1rip" />
'''RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR'''<br />
'''RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR'''<br />


==Overview==
==Overview==
The structure of ribosomal protein S17 from Bacillus stearothermophilus, was investigated by two-dimensional homonuclear and heteronuclear magnetic, resonance spectroscopy. The 1H and 15N chemical shift assignments are, largely complete, and a preliminary structural characterization is, presented. The protein consists of five beta-strands that form a single, antiparallel beta-sheet with Greek-key topology. The beta-strands are, connected by several extended loops, and two of these contain residue, types that are frequently seen in the RNA-binding sites of proteins., Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two, regions of the protein. Since these potential RNA-binding sites are, distributed over a large surface of the protein, it appears that the, molecule may interact with several regions of 16S rRNA.
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a preliminary structural characterization is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-strands are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of proteins. Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two regions of the protein. Since these potential RNA-binding sites are distributed over a large surface of the protein, it appears that the molecule may interact with several regions of 16S rRNA.


==About this Structure==
==About this Structure==
1RIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RIP OCA].  
1RIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIP OCA].  


==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Golden, B.L.]]
[[Category: Golden, B L.]]
[[Category: Hoffman, D.W.]]
[[Category: Hoffman, D W.]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan, V.]]
[[Category: White, S.W.]]
[[Category: White, S W.]]
[[Category: ribosomal protein]]
[[Category: ribosomal protein]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:18 2008''