View source for 6jq4


==HIGA Escherichia coli-K12==
<StructureSection load='6jq4' size='340' side='right'caption='[[6jq4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jq4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQ4 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&#8491;</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=6jq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jq4 OCA], [https://pdbe.org/6jq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jq4 RCSB], [https://www.ebi.ac.uk/pdbsum/6jq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jq4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HIGA_ECOLI HIGA_ECOLI] Antitoxin component of a toxin-antitoxin (TA) module. Functions as an mRNA interferase antitoxin; overexpression prevents HigB-mediated cessation of cell growth and inhibition of cell proliferation.<ref>PMID:19943910</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HigA functions as the antitoxin in HigB-HigA toxin-antitoxin system. It neutralizes HigB-mediated toxicity by forming a stable toxin-antitoxin complex. Here the crystal structure of isolated HigA from Escherichia coli str. K-12 has been determined to 2.0A resolution. The structural differences between HigA and HigA in HigBA complex imply that HigA undergoes drastic conformational changes upon the binding of HigB. The conformational changes are achieved by rigid motions of N-terminal and C-terminal domains of HigA around its central linker domain, which is different from other known forms of regulation patterns in other organisms. As a transcriptional regulator, HigA bind to its operator DNA through the C-terminal HTH motif, in which key residues were identified in this study.

Conformational changes of antitoxin HigA from Escherichia coli str. K-12 upon binding of its cognate toxin HigB reveal a new regulation mechanism in toxin-antitoxin systems.,Xu BS, Liu M, Zhou K, Geng Z, Gao ZQ, Dong YH, She Z, Liu QS Biochem Biophys Res Commun. 2019 Apr 20. pii: S0006-291X(19)30689-8. doi:, 10.1016/j.bbrc.2019.04.061. PMID:31014676<ref>PMID:31014676</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jq4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: She Z]]
[[Category: Xu BS]]