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| | ==Crystal structure of the N-terminal domain of Burkholderia Pseudomallei antitoxin HicB== | | ==Crystal structure of the N-terminal domain of Burkholderia Pseudomallei antitoxin HicB== |
| - | <StructureSection load='6g1c' size='340' side='right' caption='[[6g1c]], [[Resolution|resolution]] 1.56Å' scene=''> | + | <StructureSection load='6g1c' size='340' side='right'caption='[[6g1c]], [[Resolution|resolution]] 1.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6g1c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burps Burps]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_K96243 Burkholderia pseudomallei K96243]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G1C FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BPSS0391 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272560 BURPS])</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]] 1.56Å</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=6g1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g1c OCA], [http://pdbe.org/6g1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g1c RCSB], [http://www.ebi.ac.uk/pdbsum/6g1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g1c 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=6g1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g1c OCA], [https://pdbe.org/6g1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g1c RCSB], [https://www.ebi.ac.uk/pdbsum/6g1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g1c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q63NA5_BURPS Q63NA5_BURPS] |
| | <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: Burps]] | + | [[Category: Burkholderia pseudomallei K96243]] |
| - | [[Category: Crump, M P]] | + | [[Category: Large Structures]] |
| - | [[Category: Williams, C]] | + | [[Category: Crump MP]] |
| - | [[Category: Winter, A J]] | + | [[Category: Williams C]] |
| - | [[Category: Antitoxin]] | + | [[Category: Winter AJ]] |
| - | [[Category: N-terminal domain of the antitoxin hicb which acts as an inhibitor to hica]]
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| Structural highlights
Function
Q63NA5_BURPS
Publication Abstract from PubMed
Toxin-antitoxin (TA) systems are present in many bacteria and play important roles in bacterial growth, physiology, and pathogenicity. Those that are best studied are the type II TA systems, in which both toxins and antitoxins are proteins. The HicAB system is one of the prototypic TA systems, found in many bacterial species. Complex interactions between the protein toxin (HicA), the protein antitoxin (HicB), and the DNA upstream of the encoding genes regulate the activity of this system, but few structural details are available about how HicA destabilizes the HicB-DNA complex. Here, we determined the X-ray structures of HicB and the HicAB complex to 1.8 and 2.5 A resolution respectively and characterized their DNA interactions. This revealed that HicB forms a tetramer and HicA and HicB form a hetero-octameric complex that involves structural reorganization of the C-terminal (DNA-binding) region of HicB. Our observations indicated that HicA has a profound impact on binding of HicB to DNA sequences upstream of hicAB in a stoichiometric-dependent way. At low ratios of HicA:HicB, there was no effect on DNA binding, but at higher ratios, the affinity for DNA declined cooperatively, driving dissociation of the HicA:HicB:DNA complex.These results reveal the structural mechanisms by which HicA de-represses the HicB-DNA complex.
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA.,Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP J Biol Chem. 2018 Oct 18. pii: RA118.005173. doi: 10.1074/jbc.RA118.005173. PMID:30337369[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP. The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA. J Biol Chem. 2018 Oct 18. pii: RA118.005173. doi: 10.1074/jbc.RA118.005173. PMID:30337369 doi:http://dx.doi.org/10.1074/jbc.RA118.005173
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