6hpc: Difference between revisions

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'''Unreleased structure'''


The entry 6hpc is ON HOLD  until Paper Publication
==Crystal structure of the HicB antitoxin from E. coli==
<StructureSection load='6hpc' size='340' side='right'caption='[[6hpc]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</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='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>
</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;">
== 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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 DE]]
[[Category: Manav MC]]
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