4O7K

Crystal structure of Oncogenic Suppression Activity Protein - A Plasmid Fertility Inhibition Factor

Summary for 4O7K

• Entry DOI: 10.2210/pdb4o7k/pdb
• Related: 4OVB
• Descriptor: Protein osa, PHOSPHATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: plasmid fertility inhibition, antitumor protein
• Biological source: Shigella flexneri
• Total number of polymer chains: 1
• Total formula weight: 21623.27

Authors

Maindola, P.,Goyal, P.,Arulandu, A. (deposition date: 2013-12-25, release date: 2014-11-05, Last modification date: 2024-03-20)

Primary citation

Maindola, P.,Raina, R.,Goyal, P.,Atmakuri, K.,Ojha, A.,Gupta, S.,Christie, P.J.,Iyer, L.M.,Aravind, L.,Arockiasamy, A.
Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids
Nat Commun, 5:5322-5322, 2014

PubMed Abstract: Conjugative plasmids are typically locked in intergenomic and sexual conflicts with co-resident rivals, whose translocation they block using fertility inhibition factors (FINs). We describe here the first crystal structure of an enigmatic FIN Osa deployed by the proteobacterial plasmid pSa. Osa contains a catalytically active version of the ParB/Sulfiredoxin fold with both ATPase and DNase activity, the latter being regulated by an ATP-dependent switch. Using the Agrobacterium tumefaciens VirB/D4 type IV secretion system (T4SS), a relative of the conjugative T4SS, we demonstrate that catalytically active Osa blocks T-DNA transfer into plants. With a partially reconstituted T4SS in vitro, we show that Osa degrades T-DNA in the T-DNA-VirD2 complex before its translocation. Further, we present evidence for conservation and interplay between ATPase and DNase activities throughout the ParB/Sulfiredoxin fold, using other members of the family, namely P1 ParB and RK2 KorB, which have general functional implications across diverse biological contexts.

PubMed: 25358815
DOI: 10.1038/ncomms6322

Experimental method

X-RAY DIFFRACTION (1.748 Å)