1nmg: Difference between revisions

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[[Image:1nmg.jpg|left|200px]]<br /><applet load="1nmg" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1nmg.jpg|left|200px]]<br /><applet load="1nmg" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1nmg" />

'''MAJOR COLD-SHOCK PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />

==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.

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==

1NMG 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=1NMG OCA].

1NMG 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=1NMG OCA].

==Reference==

Line 13:

[[Category: Bacillus subtilis]]

[[Category: Single protein]]

[[Category: Holak, T.A.]]

[[Category: Holak, T A.]]

[[Category: Schnuchel, A.]]

[[Category: cold shock protein]]

[[Category: transcription regulation]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 22~~:23:~~23 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:40 2008''

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-[[Image:1nmg.jpg|left|200px]]<br /><applet load="1nmg" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nmg.jpg|left|200px]]<br /><applet load="1nmg" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nmg" />
 '''MAJOR COLD-SHOCK PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 ==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.
+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==
-NMG 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=1NMG OCA].
+NMG 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=1NMG OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Holak, T.A.]]
+[[Category: Holak, T A.]]
 [[Category: Schnuchel, A.]]
 [[Category: cold shock protein]]
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:23:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:40 2008''