1ne3

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(New page: 200px<br /><applet load="1ne3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ne3" /> '''Solution structure of ribosomal protein S28E...)
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[[Image:1ne3.gif|left|200px]]<br /><applet load="1ne3" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of ribosomal protein S28E from Methanobacterium Thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH0256_1_68; Northeast Structural Genomics Target TT744'''<br />
'''Solution structure of ribosomal protein S28E from Methanobacterium Thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH0256_1_68; Northeast Structural Genomics Target TT744'''<br />
==Overview==
==Overview==
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The ribosomal protein S28E from the archaeon Methanobacterium, thermoautotrophicum is a component of the 30S ribosomal subunit. Sequence, homologs of S28E are found only in archaea and eukaryotes. Here we report, the three-dimensional solution structure of S28E by NMR spectroscopy. S28E, contains a globular region and a long C-terminal tail protruding from the, core. The globular region consists of four antiparallel beta-strands that, are arranged in a Greek-key topology. Unique features of S28E include an, extended loop L2-3 that folds back onto the protein and a 12-residue, charged C-terminal tail with no regular secondary structure and greater, flexibility relative to the rest of the protein. The structural and, surface resemblance to OB-fold family of proteins and the presence of, highly conserved basic residues suggest that S28E may bind to RNA. A broad, positively charged surface extending over one side of the beta-barrel and, into the flexible C terminus may present a putative binding site for RNA.
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The ribosomal protein S28E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. Sequence homologs of S28E are found only in archaea and eukaryotes. Here we report the three-dimensional solution structure of S28E by NMR spectroscopy. S28E contains a globular region and a long C-terminal tail protruding from the core. The globular region consists of four antiparallel beta-strands that are arranged in a Greek-key topology. Unique features of S28E include an extended loop L2-3 that folds back onto the protein and a 12-residue charged C-terminal tail with no regular secondary structure and greater flexibility relative to the rest of the protein. The structural and surface resemblance to OB-fold family of proteins and the presence of highly conserved basic residues suggest that S28E may bind to RNA. A broad positively charged surface extending over one side of the beta-barrel and into the flexible C terminus may present a putative binding site for RNA.
==About this Structure==
==About this Structure==
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1NE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NE3 OCA].
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1NE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE3 OCA].
==Reference==
==Reference==
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[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Methanothermococcus thermolithotrophicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arrowsmith, C.H.]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Cort, J.R.]]
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[[Category: Cort, J R.]]
[[Category: Edwards, A.]]
[[Category: Edwards, A.]]
[[Category: Kennedy, M.]]
[[Category: Kennedy, M.]]
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[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
[[Category: Pineda-Lucena, A.]]
[[Category: Pineda-Lucena, A.]]
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[[Category: Ramelot, T.A.]]
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[[Category: Ramelot, T A.]]
[[Category: Wu, B.]]
[[Category: Wu, B.]]
[[Category: Yee, A.]]
[[Category: Yee, A.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:10:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:05 2008''

Revision as of 12:05, 21 February 2008


1ne3

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Solution structure of ribosomal protein S28E from Methanobacterium Thermoautotrophicum. Ontario Centre for Structural Proteomics target MTH0256_1_68; Northeast Structural Genomics Target TT744

Overview

The ribosomal protein S28E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. Sequence homologs of S28E are found only in archaea and eukaryotes. Here we report the three-dimensional solution structure of S28E by NMR spectroscopy. S28E contains a globular region and a long C-terminal tail protruding from the core. The globular region consists of four antiparallel beta-strands that are arranged in a Greek-key topology. Unique features of S28E include an extended loop L2-3 that folds back onto the protein and a 12-residue charged C-terminal tail with no regular secondary structure and greater flexibility relative to the rest of the protein. The structural and surface resemblance to OB-fold family of proteins and the presence of highly conserved basic residues suggest that S28E may bind to RNA. A broad positively charged surface extending over one side of the beta-barrel and into the flexible C terminus may present a putative binding site for RNA.

About this Structure

1NE3 is a Single protein structure of sequence from Methanothermococcus thermolithotrophicus. Full crystallographic information is available from OCA.

Reference

Solution structure of ribosomal protein S28E from Methanobacterium thermoautotrophicum., Wu B, Yee A, Pineda-Lucena A, Semesi A, Ramelot TA, Cort JR, Jung JW, Edwards A, Lee W, Kennedy M, Arrowsmith CH, Protein Sci. 2003 Dec;12(12):2831-7. PMID:14627743

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