1auu

<StructureSection load='1auu' size='340' side='right'caption='[[1auu]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1auu]] is a 2 chain structure with sequence from [https://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 [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'>[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>

[[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>

<div style="background-color:#fffaf0;">

== 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<ref>PMID:9305643</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1auu" style="background-color:#fffaf0;"></div>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Kochoyan, M]]

[[Category: Transcription regulation]]