1auu: Difference between revisions
New page: left|200px<br /><applet load="1auu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1auu" /> '''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN... |
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[[Image:1auu.gif|left|200px]]<br /><applet load="1auu" size=" | [[Image:1auu.gif|left|200px]]<br /><applet load="1auu" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
SacY is the prototype of a family of regulatory proteins able to prevent | SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction. | ||
==About this Structure== | ==About this Structure== | ||
1AUU 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:// | 1AUU 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=1AUU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:30 2008'' | ||
Revision as of 09:48, 21 February 2008
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SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES
Overview
SacY is the prototype of a family of regulatory proteins able to prevent transcription termination. It interacts with a 29 nucleotide RNA sequence able to fold into a stem-loop structure and partially overlapping with a terminator sequence located in the 5' leader mRNA region of the gene it controls. We show here that the N-terminal fragment of SacY, SacY(1-55), and the corresponding fragments of other members of the family have antiterminator activities with efficiency and specificity identical to those of the full-length proteins. In vitro, this activity correlates with the specific affinity of SacY(1-55) for its RNA target. UV melting experiments demonstrate that SacY(1-55) binding stabilizes the RNA target structure. The NMR solution structure of SacY(1-55) is very similar to that obtained in the crystal (van Tilbeurgh et al., 1997): the peptide is folded as a symmetrical dimer without any structural homology with other RNA-binding domains yet characterized. According to a preliminary NMR analysis of the SacY(1-55)-RNA complex, the protein dimer is not disrupted upon RNA binding and several residues implicated in RNA recognition are located at the edge of the dimer interface. This suggests a new mode of protein-RNA interaction.
About this Structure
1AUU is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins., Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S, EMBO J. 1997 Aug 15;16(16):5019-29. PMID:9305643
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