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4PU3

Shewanella oneidensis MR-1 Toxin Antitoxin System HipA, HipB and its operator DNA complex (space group P212121)

Summary for 4PU3
Entry DOI10.2210/pdb4pu3/pdb
Related4PU4 4PU5
DescriptorToxin-antitoxin system toxin HipA family, Toxin-antitoxin system antidote transcriptional repressor Xre family, Operator DNA, ... (4 entities in total)
Functional Keywordstoxin antitoxin system, toxin-antitoxin-dna complex, toxin/antitoxin/dna
Biological sourceShewanella oneidensis
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Total number of polymer chains6
Total formula weight144207.75
Authors
Wen, Y.,Behiels, E.,Felix, J.,Elegheert, J.,Vergauwen, B.,Devreese, B.,Savvides, S. (deposition date: 2014-03-12, release date: 2014-08-06, Last modification date: 2024-11-06)
Primary citationWen, Y.,Behiels, E.,Felix, J.,Elegheert, J.,Vergauwen, B.,Devreese, B.,Savvides, S.N.
The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence.
Nucleic Acids Res., 42:10134-10147, 2014
Cited by
PubMed Abstract: Nearly all bacteria exhibit a type of phenotypic growth described as persistence that is thought to underlie antibiotic tolerance and recalcitrant chronic infections. The chromosomally encoded high-persistence (Hip) toxin-antitoxin proteins HipASO and HipBSO from Shewanella oneidensis, a proteobacterium with unusual respiratory capacities, constitute a type II toxin-antitoxin protein module. Here we show that phosphorylated HipASO can engage in an unexpected ternary complex with HipBSO and double-stranded operator DNA that is distinct from the prototypical counterpart complex from Escherichia coli. The structure of HipBSO in complex with operator DNA reveals a flexible C-terminus that is sequestered by HipASO in the ternary complex, indicative of its role in binding HipASO to abolish its function in persistence. The structure of HipASO in complex with a non-hydrolyzable ATP analogue shows that HipASO autophosphorylation is coupled to an unusual conformational change of its phosphorylation loop. However, HipASO is unable to phosphorylate the translation factor Elongation factor Tu, contrary to previous reports, but in agreement with more recent findings. Our studies suggest that the phosphorylation state of HipA is an important factor in persistence and that the structural and mechanistic diversity of HipAB modules as regulatory factors in bacterial persistence is broader than previously thought.
PubMed: 25056321
DOI: 10.1093/nar/gku665
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.39 Å)
Structure validation

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