6hpb
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of the E.coli HicAB toxin-antitoxin complex== | |
+ | <StructureSection load='6hpb' size='340' side='right'caption='[[6hpb]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6hpb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_2-222-05_s4_c3 Escherichia coli 2-222-05_s4_c3] and [http://en.wikipedia.org/wiki/Escherichia_coli_mg1655 Escherichia coli mg1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HPB FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hpc|6hpc]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hicA, yncN, b4532, JW5230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511145 Escherichia coli MG1655]), hicB, ydcQ, b1438, JW1433 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1444264 Escherichia coli 2-222-05_S4_C3])</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=6hpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hpb OCA], [http://pdbe.org/6hpb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hpb RCSB], [http://www.ebi.ac.uk/pdbsum/6hpb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hpb ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/HICA_ECOLI HICA_ECOLI]] Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-independent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome (after 90 minutes) by subsequent expression of antitoxin HicB. Overexpression causes cleavage of a number of mRNAs and tmRNA, in a translation-independent fashion, suggesting this is an mRNA interferase (PubMed:19060138). mRNA interferases play a role in bacterial persistence to antibiotics (PubMed:21788497).<ref>PMID:19060138</ref> <ref>PMID:21788497</ref> [[http://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;"> | ||
+ | == 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<ref>PMID:31495532</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6hpb" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Escherichia coli 2-222-05_s4_c3]] | ||
+ | [[Category: Escherichia coli mg1655]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Brodersen, D E]] | ||
+ | [[Category: Manav, M C]] | ||
+ | [[Category: Dna-binding]] | ||
+ | [[Category: Protein complex]] | ||
+ | [[Category: Ta]] | ||
+ | [[Category: Ta complex]] | ||
+ | [[Category: Toxin]] | ||
+ | [[Category: Toxin-antitoxin]] |
Revision as of 11:31, 13 November 2019
Crystal structure of the E.coli HicAB toxin-antitoxin complex
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