3DD9

Structure of DocH66Y dimer

Summary for 3DD9

• Entry DOI: 10.2210/pdb3dd9/pdb
• Related: 3DD7
• Descriptor: Death on curing protein (2 entities in total)
• Functional Keywords: all alpha, ribosome inhibitor
• Biological source: Enterobacteria phage P1
• Total number of polymer chains: 8
• Total formula weight: 118260.16

Authors

Garcia-Pino, A.,Loris, R. (deposition date: 2008-06-05, release date: 2009-06-09, Last modification date: 2023-11-01)

Primary citation

De Gieter, S.,Konijnenberg, A.,Talavera, A.,Butterer, A.,Haesaerts, S.,De Greve, H.,Sobott, F.,Loris, R.,Garcia-Pino, A.
The intrinsically disordered domain of the antitoxin Phd chaperones the toxin Doc against irreversible inactivation and misfolding
J. Biol. Chem., 289:34013-34023, 2014

PubMed Abstract: The toxin Doc from the phd/doc toxin-antitoxin module targets the cellular translation machinery and is inhibited by its antitoxin partner Phd. Here we show that Phd also functions as a chaperone, keeping Doc in an active, correctly folded conformation. In the absence of Phd, Doc exists in a relatively expanded state that is prone to dimerization through domain swapping with its active site loop acting as hinge region. The domain-swapped dimer is not capable of arresting protein synthesis in vitro, whereas the Doc monomer is. Upon binding to Phd, Doc becomes more compact and is secured in its monomeric state with a neutralized active site.

PubMed: 25326388
DOI: 10.1074/jbc.M114.572396

Experimental method

X-RAY DIFFRACTION (2.45 Å)