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TitleFtsK in motion reveals its mechanism for double-stranded DNA translocation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 117, Issue 25, Page 14202-14208, Year 2020
Publish dateJun 23, 2020
AuthorsNicolas L Jean / Trevor J Rutherford / Jan Löwe /
PubMed AbstractFtsK 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:32513722 / PubMed Central
MethodsEM (single particle)
Resolution3.65 - 4.91 Å
Structure data

10399

6t8b

EMDB-10399, PDB-6t8b:
FtsK motor domain with dsDNA, translocating state
Method: EM (single particle) / Resolution: 3.65 Å

10400

6t8g

EMDB-10400, PDB-6t8g:
Stalled FtsK motor domain bound to dsDNA
Method: EM (single particle) / Resolution: 4.34 Å

10402

6t8o

EMDB-10402, PDB-6t8o:
Stalled FtsK motor domain bound to dsDNA end
Method: EM (single particle) / Resolution: 3.99 Å

EMDB-10403:
FtsK motor domain bound to dsDNA, nucleotide-free state
Method: EM (single particle) / Resolution: 4.91 Å

EMDB-10404:
FtsK motor domain bound to dsDNA, ADP-state
Method: EM (single particle) / Resolution: 4.63 Å

EMDB-10405:
FtsK motor domain bound to dsDNA, AMPPNP state
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (bacteria)
  • synthetic construct (others)
  • pseudomonas aeruginosa pao1 (bacteria)
  • unidentified (others)
KeywordsDNA BINDING PROTEIN / DNA translocation / DNA motor / RecA fold / Divisome

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