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| | ==SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES== | | ==SOLUTION STRUCTURE OF THE RNA-BINDING DOMAIN OF THE ANTITERMINATOR PROTEIN SACY, NMR, 10 STRUCTURES== |
| - | <StructureSection load='1auu' size='340' side='right' caption='[[1auu]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1auu' size='340' side='right'caption='[[1auu]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1auu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1auu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUU FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1auu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auu OCA], [http://pdbe.org/1auu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auu RCSB], [http://www.ebi.ac.uk/pdbsum/1auu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1auu ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1auu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auu OCA], [https://pdbe.org/1auu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auu RCSB], [https://www.ebi.ac.uk/pdbsum/1auu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SACY_BACSU SACY_BACSU]] In the presence of sucrose, SacY is activated and prevents premature termination of transcription by binding to a RNA-antiterminator (RAT) sequence (partially overlapping with the terminator sequence) located upstream of the sacB gene. Formation of the SacY-RAT complex prevents alternative formation of the terminator, allowing transcription of the sacB gene. In the absence of sucrose, inhibition of SacY activity by SacX leads to termination of transcription.<ref>PMID:8535520</ref> | + | [https://www.uniprot.org/uniprot/SACY_BACSU SACY_BACSU] In the presence of sucrose, SacY is activated and prevents premature termination of transcription by binding to a RNA-antiterminator (RAT) sequence (partially overlapping with the terminator sequence) located upstream of the sacB gene. Formation of the SacY-RAT complex prevents alternative formation of the terminator, allowing transcription of the sacB gene. In the absence of sucrose, inhibition of SacY activity by SacX leads to termination of transcription.<ref>PMID:8535520</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1auu_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1auu_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Kochoyan, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Antitermination]] | + | [[Category: Kochoyan M]] |
| - | [[Category: Rna binding domain]]
| + | |
| - | [[Category: Transcription regulation]]
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| Structural highlights
Function
SACY_BACSU In the presence of sucrose, SacY is activated and prevents premature termination of transcription by binding to a RNA-antiterminator (RAT) sequence (partially overlapping with the terminator sequence) located upstream of the sacB gene. Formation of the SacY-RAT complex prevents alternative formation of the terminator, allowing transcription of the sacB gene. In the absence of sucrose, inhibition of SacY activity by SacX leads to termination of transcription.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tortosa P, Le Coq D. A ribonucleic antiterminator sequence (RAT) and a distant palindrome are both involved in sucrose induction of the Bacillus subtilis sacXY regulatory operon. Microbiology. 1995 Nov;141 ( Pt 11):2921-7. PMID:8535520
- ↑ Manival X, Yang Y, Strub MP, Kochoyan M, Steinmetz M, Aymerich S. From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins. EMBO J. 1997 Aug 15;16(16):5019-29. PMID:9305643 doi:10.1093/emboj/16.16.5019
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