1fow

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(New page: 200px<br /><applet load="1fow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fow" /> '''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOM...)
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[[Image:1fow.gif|left|200px]]<br /><applet load="1fow" size="350" color="white" frame="true" align="right" spinBox="true"
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'''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE'''<br />
'''NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE'''<br />
==Overview==
==Overview==
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The structure of the C-terminal RNA recognition domain of ribosomal, protein L11 has been solved by heteronuclear three-dimensional nuclear, magnetic resonance spectroscopy. Although the structure can be considered, high resolution in the core, 15 residues between helix alpha 1 and strand, beta 1 form an extended, unstructured loop. 15N transverse relaxation, measurements suggest that the loop is moving on a picosecond-to-nanosecond, time scale in the free protein but not in the protein bound to RNA., Chemical shifts differences between the free protein and the bound protein, suggest that the loop as well as the C-terminal end of helix alpha 3 are, involved in RNA binding.
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The structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.
==About this Structure==
==About this Structure==
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1FOW 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=1FOW OCA].
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1FOW 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=1FOW OCA].
==Reference==
==Reference==
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Draper, D.E.]]
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[[Category: Draper, D E.]]
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[[Category: Hinck, A.P.]]
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[[Category: Hinck, A P.]]
[[Category: Huang, S.]]
[[Category: Huang, S.]]
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[[Category: Markus, M.A.]]
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[[Category: Markus, M A.]]
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[[Category: Torchia, D.A.]]
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[[Category: Torchia, D A.]]
[[Category: alpha-helical protein]]
[[Category: alpha-helical protein]]
[[Category: homeodomain fold]]
[[Category: homeodomain fold]]
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[[Category: rna-binding domain]]
[[Category: rna-binding domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:06:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:57 2008''

Revision as of 10:40, 21 February 2008


1fow

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NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE

Overview

The structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.

About this Structure

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

Reference

High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA., Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA, Nat Struct Biol. 1997 Jan;4(1):70-7. PMID:8989327

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