3DD9: Structure of DocH66Y dimer

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.
PDB ID: 3DD9Download
MMDB ID: 121828
PDB Deposition Date: 2008/6/5
Updated in MMDB: 2014/07
Experimental Method:
x-ray diffraction
Resolution: 2.45  Å
Source Organism:
Similar Structures:
Biological Unit for 3DD9: dimeric; determined by author and by software (PISA)
Molecular Components in 3DD9
Label Count Molecule
Proteins (2 molecules)
Death on Curing Protein(Gene symbol: doc)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB