6jq4
From Proteopedia
HIGA Escherichia coli-K12
Structural highlights
FunctionHIGA_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.[1] Publication Abstract from PubMedHigA 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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