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| | <StructureSection load='6hpc' size='340' side='right'caption='[[6hpc]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='6hpc' size='340' side='right'caption='[[6hpc]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hpc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_2-210-07_s3_c3 Escherichia coli 2-210-07_s3_c3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hpc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_2-210-07_S3_C3 Escherichia coli 2-210-07_S3_C3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HPC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hpb|6hpb]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hicB, AC45_3823 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1444180 Escherichia coli 2-210-07_S3_C3])</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=6hpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hpc OCA], [https://pdbe.org/6hpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hpc RCSB], [https://www.ebi.ac.uk/pdbsum/6hpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hpc 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=6hpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hpc OCA], [http://pdbe.org/6hpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hpc RCSB], [http://www.ebi.ac.uk/pdbsum/6hpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hpc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HICB_ECOLI HICB_ECOLI] Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents HicA-mediated cessation of cell growth and inhibition of cell proliferation.<ref>PMID:19060138</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: Escherichia coli 2-210-07_s3_c3]] | + | [[Category: Escherichia coli 2-210-07_S3_C3]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brodersen, D E]] | + | [[Category: Brodersen DE]] |
| - | [[Category: Manav, M C]] | + | [[Category: Manav MC]] |
| - | [[Category: Antitoxin]]
| + | |
| - | [[Category: Dna binding]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Hth]]
| + | |
| Structural highlights
Function
HICB_ECOLI Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents HicA-mediated cessation of cell growth and inhibition of cell proliferation.[1]
Publication Abstract from PubMed
The E. coli hicAB type II toxin-antitoxin locus is unusual by being controlled by two promoters and by having the toxin encoded upstream of the antitoxin. HicA toxins contain a double-stranded RNA-binding fold and cleaves both mRNA and tmRNA in vivo, while HicB antitoxins contain a partial RNase H fold and either a helix-turn-helix (HTH) or ribbon-helix-helix domain. It is not known how an HTH DNA-binding domain affects higher-order structure for the HicAB modules. Here, we present crystal structures of the isolated E. coli HicB antitoxin and full-length HicAB complex showing that HicB forms a stable DNA-binding module and interacts in a canonical way with HicA despite the presence of an HTH-type DNA-binding domain. No major structural rearrangements take place upon binding of the toxin. Both structures expose well-ordered DNA-binding motifs allowing a model for DNA binding by the antitoxin to be generated.
The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain.,Manav MC, Turnbull KJ, Jurenas D, Garcia-Pino A, Gerdes K, Brodersen DE Structure. 2019 Sep 4. pii: S0969-2126(19)30279-5. doi:, 10.1016/j.str.2019.08.008. PMID:31495532[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jorgensen MG, Pandey DP, Jaskolska M, Gerdes K. HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea. J Bacteriol. 2009 Feb;191(4):1191-9. doi: 10.1128/JB.01013-08. Epub 2008 Dec 5. PMID:19060138 doi:http://dx.doi.org/10.1128/JB.01013-08
- ↑ Manav MC, Turnbull KJ, Jurenas D, Garcia-Pino A, Gerdes K, Brodersen DE. The E. coli HicB Antitoxin Contains a Structurally Stable Helix-Turn-Helix DNA Binding Domain. Structure. 2019 Sep 4. pii: S0969-2126(19)30279-5. doi:, 10.1016/j.str.2019.08.008. PMID:31495532 doi:http://dx.doi.org/10.1016/j.str.2019.08.008
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