6ww6: Difference between revisions
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==== | ==Crystal structure of EutV bound to RNA== | ||
<StructureSection load='6ww6' size='340' side='right'caption='[[6ww6]]' scene=''> | <StructureSection load='6ww6' size='340' side='right'caption='[[6ww6]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[6ww6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WW6 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=6ww6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww6 OCA], [https://pdbe.org/6ww6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ww6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ww6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww6 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene></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=6ww6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ww6 OCA], [https://pdbe.org/6ww6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ww6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ww6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ww6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1Q1FU69_ENTFL A0A1Q1FU69_ENTFL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Regulated transcription termination provides an efficient and responsive means to control gene expression. In bacteria, rho-independent termination occurs through the formation of an intrinsic RNA terminator loop, which disrupts the RNA polymerase elongation complex, resulting in its dissociation from the DNA template. Bacteria have a number of pathways for overriding termination, one of which is the formation of mutually exclusive RNA motifs. ANTAR domains are a class of antiterminator that bind and stabilize dual hexaloop RNA motifs within the nascent RNA chain to prevent terminator loop formation. We have determined the structures of the dimeric ANTAR domain protein EutV, from Enterococcus faecialis, in the absence of and in complex with the dual hexaloop RNA target. The structures illustrate conformational changes that occur upon RNA binding and reveal that the molecular interactions between the ANTAR domains and RNA are restricted to a single hexaloop of the motif. An ANTAR domain dimer must contact each hexaloop of the dual hexaloop motif individually to prevent termination in eubacteria. Our findings thereby redefine the minimal ANTAR domain binding motif to a single hexaloop and revise the current model for ANTAR-mediated antitermination. These insights will inform and facilitate the discovery of novel ANTAR domain RNA targets. | |||
Structural characterization of the ANTAR antiterminator domain bound to RNA.,Walshe JL, Siddiquee R, Patel K, Ataide SF Nucleic Acids Res. 2022 Mar 21;50(5):2889-2904. doi: 10.1093/nar/gkac074. PMID:35150565<ref>PMID:35150565</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ww6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Response regulator 3D structure|Response regulator 3D structure]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterococcus faecalis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ataide SF]] | ||
[[Category: Walshe JL]] | |||
Revision as of 09:21, 26 October 2022
Crystal structure of EutV bound to RNACrystal structure of EutV bound to RNA
Structural highlights
FunctionPublication Abstract from PubMedRegulated transcription termination provides an efficient and responsive means to control gene expression. In bacteria, rho-independent termination occurs through the formation of an intrinsic RNA terminator loop, which disrupts the RNA polymerase elongation complex, resulting in its dissociation from the DNA template. Bacteria have a number of pathways for overriding termination, one of which is the formation of mutually exclusive RNA motifs. ANTAR domains are a class of antiterminator that bind and stabilize dual hexaloop RNA motifs within the nascent RNA chain to prevent terminator loop formation. We have determined the structures of the dimeric ANTAR domain protein EutV, from Enterococcus faecialis, in the absence of and in complex with the dual hexaloop RNA target. The structures illustrate conformational changes that occur upon RNA binding and reveal that the molecular interactions between the ANTAR domains and RNA are restricted to a single hexaloop of the motif. An ANTAR domain dimer must contact each hexaloop of the dual hexaloop motif individually to prevent termination in eubacteria. Our findings thereby redefine the minimal ANTAR domain binding motif to a single hexaloop and revise the current model for ANTAR-mediated antitermination. These insights will inform and facilitate the discovery of novel ANTAR domain RNA targets. Structural characterization of the ANTAR antiterminator domain bound to RNA.,Walshe JL, Siddiquee R, Patel K, Ataide SF Nucleic Acids Res. 2022 Mar 21;50(5):2889-2904. doi: 10.1093/nar/gkac074. PMID:35150565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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