6hpc: Difference between revisions
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==Crystal structure of the HicB antitoxin from E. coli== | |||
<StructureSection load='6hpc' size='340' side='right'caption='[[6hpc]], [[Resolution|resolution]] 2.26Å' scene=''> | |||
== 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> | |||
</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">[[6hpb|6hpb]]</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'>[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> | |||
<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 6hpc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli 2-210-07_s3_c3]] | |||
[[Category: Large Structures]] | |||
[[Category: Brodersen, D E]] | |||
[[Category: Manav, M C]] | |||
[[Category: Antitoxin]] | |||
[[Category: Dna binding]] | |||
[[Category: Helix-turn-helix]] | |||
[[Category: Hth]] | |||
Revision as of 07:15, 16 October 2019
Crystal structure of the HicB antitoxin from E. coli
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