6T8G

Stalled FtsK motor domain bound to dsDNA

Summary for 6T8G

• Entry DOI: 10.2210/pdb6t8g/pdb
• Related: 6T8B 6T8O
• EMDB information: 10400
• Descriptor: DNA translocase FtsK, dsDNA substrate, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: dna translocation, dna motor, reca fold, divisome, dna binding protein
• Biological source: Pseudomonas aeruginosa PAO1; More
• Total number of polymer chains: 8
• Total formula weight: 336360.33

Authors

Jean, N.L.,Lowe, J. (deposition date: 2019-10-24, release date: 2019-11-20, Last modification date: 2024-05-22)

Primary citation

Jean, N.L.,Rutherford, T.J.,Lowe, J.
FtsK in motion reveals its mechanism for double-stranded DNA translocation.
Proc.Natl.Acad.Sci.USA, 117:14202-14208, 2020

PubMed Abstract: FtsK protein contains a fast DNA motor that is involved in bacterial chromosome dimer resolution. During cell division, FtsK translocates double-stranded DNA until both recombination sites are placed at mid cell for subsequent dimer resolution. Here, we solved the 3.6-Å resolution electron cryo-microscopy structure of the motor domain of FtsK while translocating on its DNA substrate. Each subunit of the homo-hexameric ring adopts a unique conformation and one of three nucleotide states. Two DNA-binding loops within four subunits form a pair of spiral staircases within the ring, interacting with the two DNA strands. This suggests that simultaneous conformational changes in all ATPase domains at each catalytic step generate movement through a mechanism related to filament treadmilling. While the ring is only rotating around the DNA slowly, it is instead the conformational states that rotate around the ring as the DNA substrate is pushed through.

PubMed: 32513722
DOI: 10.1073/pnas.2001324117

Experimental method

ELECTRON MICROSCOPY (4.34 Å)