1WMI
Crystal structure of archaeal RelE-RelB complex from Pyrococcus horikoshii OT3
Summary for 1WMI
| Entry DOI | 10.2210/pdb1wmi/pdb |
| Descriptor | hypothetical protein PHS013, hypothetical protein PHS014 (3 entities in total) |
| Functional Keywords | toxin-antitoxin complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Pyrococcus horikoshii More |
| Total number of polymer chains | 4 |
| Total formula weight | 37815.62 |
| Authors | Takagi, H.,Kakuta, Y.,Kamachi, R.,Yao, M.,Tanaka, I.,Kimura, M. (deposition date: 2004-07-09, release date: 2005-03-15, Last modification date: 2024-03-13) |
| Primary citation | Takagi, H.,Kakuta, Y.,Okada, T.,Yao, M.,Tanaka, I.,Kimura, M. Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects Nat.Struct.Mol.Biol., 12:327-331, 2005 Cited by PubMed Abstract: 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. PubMed: 15768033DOI: 10.1038/nsmb911 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
