3DD7
Structure of DocH66Y in complex with the C-terminal domain of Phd
Summary for 3DD7
| Entry DOI | 10.2210/pdb3dd7/pdb |
| Related | 3DD9 |
| Descriptor | Death on curing protein, Prevent host death protein, BROMIDE ION, ... (4 entities in total) |
| Functional Keywords | all alpha, ribosome inhibitor |
| Biological source | Enterobacteria phage P1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 36116.95 |
| Authors | Garcia-Pino, A.,Loris, R. (deposition date: 2008-06-05, release date: 2008-09-16, Last modification date: 2024-11-06) |
| Primary citation | Garcia-Pino, A.,Christensen-Dalsgaard, M.,Wyns, L.,Yarmolinsky, M.,Magnuson, R.D.,Gerdes, K.,Loris, R. Doc of Prophage P1 Is Inhibited by Its Antitoxin Partner Phd through Fold Complementation J.Biol.Chem., 283:30821-30827, 2008 Cited by PubMed Abstract: Prokaryotic toxin-antitoxin modules are involved in major physiological events set in motion under stress conditions. The toxin Doc (death on curing) from the phd/doc module on phage P1 hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation. This Phd domain is intrinsically disordered in solution and folds into an alpha-helix upon binding to Doc. The details of the interactions reveal the molecular basis for the inhibitory action of the antitoxin. The complex resembles the Fic (filamentation induced by cAMP) proteins and suggests a possible evolutionary origin for the phd/doc operon. Doc induces growth arrest of Escherichia coli cells in a reversible manner, by targeting the protein synthesis machinery. Moreover, Doc activates the endogenous E. coli RelE mRNA interferase but does not require this or any other known chromosomal toxin-antitoxin locus for its action in vivo. PubMed: 18757857DOI: 10.1074/jbc.M805654200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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