2AN7

Solution structure of the bacterial antidote ParD

Summary for 2AN7

• Entry DOI: 10.2210/pdb2an7/pdb
• NMR Information: BMRB: 4792
• Descriptor: Protein parD (1 entity in total)
• Functional Keywords: bacterial antidote, ribbon-helix-helix, dna-binding motif, plasmid addiction, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 18228.50

Authors

Oberer, M.,Zangger, K.,Gruber, K.,Keller, W. (deposition date: 2005-08-11, release date: 2006-09-05, Last modification date: 2024-05-15)

Primary citation

Oberer, M.,Zangger, K.,Gruber, K.,Keller, W.
The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding.
Protein Sci., 16:1676-1688, 2007

PubMed Abstract: ParD is the antidote of the plasmid-encoded toxin-antitoxin (TA) system ParD-ParE. These modules rely on differential stabilities of a highly expressed but labile antidote and a stable toxin expressed from one operon. Consequently, loss of the coding plasmid results in loss of the protective antidote and poisoning of the cell. The antidote protein usually also exhibits an autoregulatory function of the operon. In this paper, we present the solution structure of ParD. The repressor activity of ParD is mediated by the N-terminal half of the protein, which adopts a ribbon-helix-helix (RHH) fold. The C-terminal half of the protein is unstructured in the absence of its cognate binding partner ParE. Based on homology with other RHH proteins, we present a model of the ParD-DNA interaction, with the antiparallel beta-strand being inserted into the major groove of DNA. The fusion of the N-terminal DNA-binding RHH motif to the toxin-binding unstructured C-terminal domain is discussed in its evolutionary context.

PubMed: 17656583
DOI: 10.1110/ps.062680707

Experimental method

SOLUTION NMR