1rip

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(New page: 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="350" color="white" frame="true" align="right" spinBox="true"
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'''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==
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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.
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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==
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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].
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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]]
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[[Category: Golden, B.L.]]
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[[Category: Golden, B L.]]
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[[Category: Hoffman, D.W.]]
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[[Category: Hoffman, D W.]]
[[Category: Ramakrishnan, V.]]
[[Category: Ramakrishnan, V.]]
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[[Category: White, S.W.]]
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[[Category: White, S W.]]
[[Category: ribosomal protein]]
[[Category: ribosomal protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:37:44 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:18 2008''

Revision as of 12:51, 21 February 2008


1rip

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RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR

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.

About this Structure

1RIP is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR., Golden BL, Hoffman DW, Ramakrishnan V, White SW, Biochemistry. 1993 Nov 30;32(47):12812-20. PMID:8251502

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