1wmi
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Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3
OverviewOverview
The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin, RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the, antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon, Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here, we report the crystal structure of aRelE in complex with aRelB determined, at a resolution of 2.3 A. aRelE folds into an alpha/beta structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps, around the molecular surface of aRelE. Neither component shows structural, homology to known ribonucleases or their inhibitors. Site-directed, mutagenesis suggests that Arg85, in the C-terminal region, is strongly, involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58, and Arg65 play a modest role in the toxin's activity.
About this StructureAbout this Structure
1WMI is a Protein complex structure of sequences from Pyrococcus horikoshii ot3. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects., Takagi H, Kakuta Y, Okada T, Yao M, Tanaka I, Kimura M, Nat Struct Mol Biol. 2005 Apr;12(4):327-31. Epub 2005 Mar 13. PMID:15768033
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