8RAY

ParA in complex with ATP

Summary for 8RAY

• Entry DOI: 10.2210/pdb8ray/pdb
• Descriptor: ParA family protein, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: soj, dna replication, replication
• Biological source: Myxococcus xanthus DK 1622
• Total number of polymer chains: 2
• Total formula weight: 57135.56

Authors

Mais, C.-N.,Bange, G. (deposition date: 2023-12-01, release date: 2025-03-26, Last modification date: 2025-10-08)

Primary citation

Schnabel, L.,Osorio-Valeriano, M.,Perez-Borrajero, C.,Steinchen, W.,Mais, C.N.,Simon, B.,Hanssmann, J.,Thamm, M.,Hennig, J.,Bange, G.,Thanbichler, M.
Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation.
Nat Commun, 16:8428-8428, 2025

PubMed Abstract: DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associates with a conserved bipartite binding pocket at the ParA dimer interface, in a manner dependent on ParB clamp closure. Moreover, we show that ParB and non-specific DNA interact cooperatively with ParA and synergistically induce structural changes in its Walker A and Walker B motifs that correlate with the activation of ParA ATPase activity. These results advance our understanding of the mechanism underlying DNA transport by the ParABS system and may help to unravel the mode of action of related cargo-positioning systems.

PubMed: 40998818
DOI: 10.1038/s41467-025-63976-0

Experimental method

X-RAY DIFFRACTION (1.58 Å)