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| | <StructureSection load='6chv' size='340' side='right'caption='[[6chv]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='6chv' size='340' side='right'caption='[[6chv]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6chv]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29905 Atcc 29905]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CHV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6chv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CHV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">higA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585 ATCC 29905])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chv OCA], [http://pdbe.org/6chv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6chv RCSB], [http://www.ebi.ac.uk/pdbsum/6chv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6chv ProSAT]</span></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=6chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chv OCA], [https://pdbe.org/6chv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6chv RCSB], [https://www.ebi.ac.uk/pdbsum/6chv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6chv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIGA_PROVU HIGA_PROVU]] Antitoxin component of a type II toxin-antitoxin (TA) system that counteracts the effect of the HigB toxin (PubMed:19423702, PubMed:8645296, PubMed:24257752). Binds to its own promoter and regulates transcription of the higB/higA operon (PubMed:24257752).<ref>PMID:19423702</ref> <ref>PMID:24257752</ref> <ref>PMID:8645296</ref> | + | [https://www.uniprot.org/uniprot/HIGA_PROVU HIGA_PROVU] Antitoxin component of a type II toxin-antitoxin (TA) system that counteracts the effect of the HigB toxin (PubMed:19423702, PubMed:8645296, PubMed:24257752). Binds to its own promoter and regulates transcription of the higB/higA operon (PubMed:24257752).<ref>PMID:19423702</ref> <ref>PMID:24257752</ref> <ref>PMID:8645296</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: Atcc 29905]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dunham, C M]] | + | [[Category: Proteus vulgaris]] |
| - | [[Category: Hoffer, E D]] | + | [[Category: Dunham CM]] |
| - | [[Category: Onuoha, N]] | + | [[Category: Hoffer ED]] |
| - | [[Category: Schureck, M A]] | + | [[Category: Onuoha N]] |
| - | [[Category: Antitoxin]] | + | [[Category: Schureck MA]] |
| - | [[Category: Antitoxin-dna complex]]
| + | |
| - | [[Category: Dna-protein complex]]
| + | |
| - | [[Category: Helix-turn-helix dna binding protein]]
| + | |
| - | [[Category: Toxin-antitoxin system]]
| + | |
| Structural highlights
Function
HIGA_PROVU Antitoxin component of a type II toxin-antitoxin (TA) system that counteracts the effect of the HigB toxin (PubMed:19423702, PubMed:8645296, PubMed:24257752). Binds to its own promoter and regulates transcription of the higB/higA operon (PubMed:24257752).[1] [2] [3]
Publication Abstract from PubMed
Bacterial toxin-antitoxin systems are important factors implicated in growth inhibition and plasmid maintenance. Type II toxin-antitoxin pairs are regulated at the transcriptional level by the antitoxin itself. Here, we examined how the HigA antitoxin regulates the expression of the Proteus vulgaris higBA toxin-antitoxin operon from the Rts1 plasmid. The HigBA complex adopts a unique architecture suggesting differences in its regulation as compared to classical type II toxin-antitoxin systems. We find that the C-terminus of the HigA antitoxin is required for dimerization and transcriptional repression. Further, the HigA structure reveals that the C terminus is ordered and does not transition between disorder-order states upon toxin binding. HigA residue Arg40 recognizes a TpG dinucleotide in higO2, an evolutionary conserved mode of recognition among prokaryotic and eukaryotic transcriptional factors. Comparison of the HigBA and HigA-higO2 structures reveals the distance between helix-turn-helix motifs of each HigA monomer increases by ~4 A in order to bind to higO2. Consistent with these data, HigBA binding to each operator is two-fold less tight than HigA alone. Together, these data show the HigB toxin does not act as a co-repressor suggesting potential novel regulation in this toxin-antitoxin system. This article is protected by copyright. All rights reserved.
Structural basis of transcriptional regulation by the HigA antitoxin.,Schureck MA, Meisner J, Hoffer ED, Wang D, Onuoha N, Ei Cho S, Lollar P 3rd, Dunham CM Mol Microbiol. 2019 Feb 21. doi: 10.1111/mmi.14229. PMID:30793388[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hurley JM, Woychik NA. Bacterial toxin HigB associates with ribosomes and mediates translation-dependent mRNA cleavage at A-rich sites. J Biol Chem. 2009 Jul 10;284(28):18605-13. doi: 10.1074/jbc.M109.008763. Epub, 2009 May 7. PMID:19423702 doi:http://dx.doi.org/10.1074/jbc.M109.008763
- ↑ Schureck MA, Maehigashi T, Miles SJ, Marquez J, Ei Cho S, Erdman R, Dunham CM. Structure of the P. vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem. 2013 Nov 20. PMID:24257752 doi:http://dx.doi.org/10.1074/jbc.M113.512095
- ↑ Tian QB, Ohnishi M, Tabuchi A, Terawaki Y. A new plasmid-encoded proteic killer gene system: cloning, sequencing, and analyzing hig locus of plasmid Rts1. Biochem Biophys Res Commun. 1996 Mar 18;220(2):280-4. PMID:8645296 doi:http://dx.doi.org/S0006-291X(96)90396-4
- ↑ Schureck MA, Meisner J, Hoffer ED, Wang D, Onuoha N, Ei Cho S, Lollar P 3rd, Dunham CM. Structural basis of transcriptional regulation by the HigA antitoxin. Mol Microbiol. 2019 Feb 21. doi: 10.1111/mmi.14229. PMID:30793388 doi:http://dx.doi.org/10.1111/mmi.14229
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