6tf4: Difference between revisions
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<StructureSection load='6tf4' size='340' side='right'caption='[[6tf4]]' scene=''> | <StructureSection load='6tf4' size='340' side='right'caption='[[6tf4]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full | <table><tr><td colspan='2'>[[6tf4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TF4 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=6tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tf4 OCA], [https://pdbe.org/6tf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tf4 RCSB], [https://www.ebi.ac.uk/pdbsum/6tf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tf4 ProSAT]</span></td></tr> | </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=6tf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tf4 OCA], [https://pdbe.org/6tf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tf4 RCSB], [https://www.ebi.ac.uk/pdbsum/6tf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tf4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9KTB3_VIBCH Q9KTB3_VIBCH] Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components.[HAMAP-Rule:MF_00951] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The two-domain protein RfaH, a paralog of the universally conserved NusG/Spt5 transcription factors, is regulated by autoinhibition coupled to the reversible conformational switch of its 60-residue C-terminal Kyrpides, Ouzounis, Woese (KOW) domain between an alpha-hairpin and a beta-barrel. In contrast, NusG/Spt5-KOW domains only occur in the beta-barrel state. To understand the principles underlying the drastic fold switch in RfaH, we elucidated the thermodynamic stability and the structural dynamics of two RfaH- and four NusG/Spt5-KOW domains by combining biophysical and structural biology methods. We find that the RfaH-KOW beta-barrel is thermodynamically less stable than that of most NusG/Spt5-KOWs and we show that it is in equilibrium with a globally unfolded species, which, strikingly, contains two helical regions that prime the transition toward the alpha-hairpin. Our results suggest that transiently structured elements in the unfolded conformation might drive the global folding transition in metamorphic proteins in general. | |||
Structural and thermodynamic analyses of the beta-to-alpha transformation in RfaH reveal principles of fold-switching proteins.,Zuber PK, Daviter T, Heissmann R, Persau U, Schweimer K, Knauer SH Elife. 2022 Oct 18;11:e76630. doi: 10.7554/eLife.76630. PMID:36255050<ref>PMID:36255050</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tf4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Vibrio cholerae]] | |||
[[Category: Knauer SH]] | [[Category: Knauer SH]] | ||
[[Category: Schweimer K]] | [[Category: Schweimer K]] | ||
[[Category: Zuber PK]] | [[Category: Zuber PK]] | ||
Revision as of 11:27, 7 December 2022
Solution structure of RfaH C-terminal domain from Vibrio choleraeSolution structure of RfaH C-terminal domain from Vibrio cholerae
Structural highlights
FunctionQ9KTB3_VIBCH Enhances distal genes transcription elongation in a specialized subset of operons that encode extracytoplasmic components.[HAMAP-Rule:MF_00951] Publication Abstract from PubMedThe two-domain protein RfaH, a paralog of the universally conserved NusG/Spt5 transcription factors, is regulated by autoinhibition coupled to the reversible conformational switch of its 60-residue C-terminal Kyrpides, Ouzounis, Woese (KOW) domain between an alpha-hairpin and a beta-barrel. In contrast, NusG/Spt5-KOW domains only occur in the beta-barrel state. To understand the principles underlying the drastic fold switch in RfaH, we elucidated the thermodynamic stability and the structural dynamics of two RfaH- and four NusG/Spt5-KOW domains by combining biophysical and structural biology methods. We find that the RfaH-KOW beta-barrel is thermodynamically less stable than that of most NusG/Spt5-KOWs and we show that it is in equilibrium with a globally unfolded species, which, strikingly, contains two helical regions that prime the transition toward the alpha-hairpin. Our results suggest that transiently structured elements in the unfolded conformation might drive the global folding transition in metamorphic proteins in general. Structural and thermodynamic analyses of the beta-to-alpha transformation in RfaH reveal principles of fold-switching proteins.,Zuber PK, Daviter T, Heissmann R, Persau U, Schweimer K, Knauer SH Elife. 2022 Oct 18;11:e76630. doi: 10.7554/eLife.76630. PMID:36255050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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