1nmf

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(New page: 200px<br /><applet load="1nmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nmf" /> '''MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES...)
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'''MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES'''<br />
'''MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES'''<br />
==Overview==
==Overview==
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The cold-shock domain (CSD) is found in many eukaryotic transcriptional, factors and is responsible for the specific binding to DNA of a, cis-element called the Y-box. The same domain exists in the sequence of, the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major, cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB), have sequences that are more than 40 per cent identical to the cold-shock, domain. We present here the three-dimensional structure of CspB determined, by nuclear magnetic resonance spectroscopy. The 67-residue protein, consists of an antiparallel five-stranded beta-barrel with strands, connected by turns and loops. The structure resembles that of, staphylococcal nuclease and the gene-5 single-stranded-DNA-binding, protein. A three-stranded beta-sheet, which contains the conserved, RNA-binding motif RNP1 as well as a motif similar to RNP2 in two, neighbouring antiparallel beta-strands, has basic and aromatic residues at, its surface which could serve as a binding site for single-stranded DNA., CspB binds to single-stranded DNA in gel retardation experiments.
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The cold-shock domain (CSD) is found in many eukaryotic transcriptional factors and is responsible for the specific binding to DNA of a cis-element called the Y-box. The same domain exists in the sequence of the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB) have sequences that are more than 40 per cent identical to the cold-shock domain. We present here the three-dimensional structure of CspB determined by nuclear magnetic resonance spectroscopy. The 67-residue protein consists of an antiparallel five-stranded beta-barrel with strands connected by turns and loops. The structure resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein. A three-stranded beta-sheet, which contains the conserved RNA-binding motif RNP1 as well as a motif similar to RNP2 in two neighbouring antiparallel beta-strands, has basic and aromatic residues at its surface which could serve as a binding site for single-stranded DNA. CspB binds to single-stranded DNA in gel retardation experiments.
==About this Structure==
==About this Structure==
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1NMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NMF OCA].
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1NMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMF OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Holak, T.A.]]
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[[Category: Holak, T A.]]
[[Category: Schnuchel, A.]]
[[Category: Schnuchel, A.]]
[[Category: cold shock protein]]
[[Category: cold shock protein]]
[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:23:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:38 2008''

Revision as of 12:07, 21 February 2008


1nmf

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MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES

Overview

The cold-shock domain (CSD) is found in many eukaryotic transcriptional factors and is responsible for the specific binding to DNA of a cis-element called the Y-box. The same domain exists in the sequence of the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB) have sequences that are more than 40 per cent identical to the cold-shock domain. We present here the three-dimensional structure of CspB determined by nuclear magnetic resonance spectroscopy. The 67-residue protein consists of an antiparallel five-stranded beta-barrel with strands connected by turns and loops. The structure resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein. A three-stranded beta-sheet, which contains the conserved RNA-binding motif RNP1 as well as a motif similar to RNP2 in two neighbouring antiparallel beta-strands, has basic and aromatic residues at its surface which could serve as a binding site for single-stranded DNA. CspB binds to single-stranded DNA in gel retardation experiments.

About this Structure

1NMF is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structure in solution of the major cold-shock protein from Bacillus subtilis., Schnuchel A, Wiltscheck R, Czisch M, Herrler M, Willimsky G, Graumann P, Marahiel MA, Holak TA, Nature. 1993 Jul 8;364(6433):169-71. PMID:8321289

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