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| | <StructureSection load='6gho' size='340' side='right'caption='[[6gho]], [[Resolution|resolution]] 1.79Å' scene=''> | | <StructureSection load='6gho' size='340' side='right'caption='[[6gho]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6gho]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu] and [http://en.wikipedia.org/wiki/Geoka Geoka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GHO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gho]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168] and [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GHO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ghb|6ghb]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spxA, yjbD, BSU11500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), GK0824 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235909 GEOKA])</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=6gho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gho OCA], [https://pdbe.org/6gho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gho RCSB], [https://www.ebi.ac.uk/pdbsum/6gho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gho ProSAT]</span></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=6gho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gho OCA], [http://pdbe.org/6gho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gho RCSB], [http://www.ebi.ac.uk/pdbsum/6gho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gho ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SPX_BACSU SPX_BACSU]] Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development-promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development.<ref>PMID:11703662</ref> <ref>PMID:12642660</ref> | + | [https://www.uniprot.org/uniprot/SPX_BACSU SPX_BACSU] Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development-promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development.<ref>PMID:11703662</ref> <ref>PMID:12642660</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Geoka]] | + | [[Category: Geobacillus kaustophilus HTA426]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Awad, W]] | + | [[Category: Awad W]] |
| - | [[Category: Logan, D T]] | + | [[Category: Logan DT]] |
| - | [[Category: Wachenfeldt, C von]] | + | [[Category: Von Wachenfeldt C]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Regulatory protein spx adaptor protein yjbh]]
| + | |
| Structural highlights
Function
SPX_BACSU Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development-promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development.[1] [2]
Publication Abstract from PubMed
YjbH is a bacterial adaptor protein required for efficient proteolysis of the RNA polymerase-binding transcription factor Spx by the ClpXP protease. We report the structure of YjbH in complex with Spx. YjbH comprises a DsbA-like thioredoxin domain connected via a linker to a C-terminal domain reminiscent of the winged helix-turn-helix fold. The interaction between YjbH and Spx involves a large surface area. Binding to YjbH stabilizes the C-terminal ClpX recognition region of Spx. We show that mutation of critical YjbH contact residues abrogates Spx recognition. Small-angle X-ray scattering and hydrogen-deuterium exchange mass spectrometry analyses determined the existence of a stable heterodimeric complex in solution and provide evidence that binding of Spx to YjbH reduces the overall conformational flexibility of Spx. Our findings provide insights into the molecular basis for Spx recognition and suggest a model for how YjbH stabilizes Spx and displays the C terminus of Spx for engagement by ClpXP.
Structural Basis for YjbH Adaptor-Mediated Recognition of Transcription Factor Spx.,Awad W, Al-Eryani Y, Ekstrom S, Logan DT, von Wachenfeldt C Structure. 2019 Apr 3. pii: S0969-2126(19)30087-5. doi:, 10.1016/j.str.2019.03.009. PMID:30982633[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakano MM, Hajarizadeh F, Zhu Y, Zuber P. Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent competence development of Bacillus subtilis. Mol Microbiol. 2001 Oct;42(2):383-94. PMID:11703662
- ↑ Nakano S, Nakano MM, Zhang Y, Leelakriangsak M, Zuber P. A regulatory protein that interferes with activator-stimulated transcription in bacteria. Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):4233-8. Epub 2003 Mar 17. PMID:12642660 doi:http://dx.doi.org/10.1073/pnas.0637648100
- ↑ Awad W, Al-Eryani Y, Ekstrom S, Logan DT, von Wachenfeldt C. Structural Basis for YjbH Adaptor-Mediated Recognition of Transcription Factor Spx. Structure. 2019 Apr 3. pii: S0969-2126(19)30087-5. doi:, 10.1016/j.str.2019.03.009. PMID:30982633 doi:http://dx.doi.org/10.1016/j.str.2019.03.009
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