4pu4

Shewanella oneidensis MR-1 Toxin Antitoxin System HipA, HipB and its operator DNA complex (space group P21)

spinqualitylabelsall models 4pu4, resolution 3.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pu4 is a 6 chain structure with sequence from Shewanella oneidensis and Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.786Å Ligands: SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HIPA_SHEON Toxic component of a type II toxin-antitoxin (TA) system; overexpression in wild-type temporarily inhibits cell growth, overexpression in a hipAB deletion leads to acute growth inhibition. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. In the ternary phosphoserine-HipA-HipB-DNA complex the DNA is bent about 125 degrees; all HipA in the crystallized ternary complex is phosphorylated. In E.coli phosphorylation of HipA is thought to release HipB from the HipA-HipB-DNA complex, suggesting the complex functions differently in the 2 bacteria (PubMed:25056321). Phosphorylates Glu-tRNA-ligase (GltX, on 'Ser-239') in vivo, with HipB probably acts as a corepressor for transcription of the hipBA promoter (By similarity).[UniProtKB:P23874] Publication Abstract from PubMed 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. The bacterial antitoxin HipB establishes a ternary complex with operator DNA and phosphorylated toxin HipA to regulate bacterial persistence.,Wen Y, Behiels E, Felix J, Elegheert J, Vergauwen B, Devreese B, Savvides SN Nucleic Acids Res. 2014 Jul 23. pii: gku665. PMID:25056321 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase 3D structures

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