6cf1
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Proteus vulgaris HigA antitoxin structure== | ==Proteus vulgaris HigA antitoxin structure== | ||
| - | <StructureSection load='6cf1' size='340' side='right' caption='[[6cf1]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6cf1' size='340' side='right'caption='[[6cf1]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6cf1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CF1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cf1]] is a 2 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=6CF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CF1 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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='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=6cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cf1 OCA], [http://pdbe.org/6cf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cf1 RCSB], [http://www.ebi.ac.uk/pdbsum/6cf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cf1 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=6cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cf1 OCA], [http://pdbe.org/6cf1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cf1 RCSB], [http://www.ebi.ac.uk/pdbsum/6cf1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cf1 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:30793388</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6cf1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 29905]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Cho, S Ei]] | [[Category: Cho, S Ei]] | ||
[[Category: Dunham, C M]] | [[Category: Dunham, C M]] | ||
Revision as of 12:36, 13 March 2019
Proteus vulgaris HigA antitoxin structure
| |||||||||||
