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PMID:16916635
| Citation |
Massey, TH, Mercogliano, CP, Yates, J, Sherratt, DJ and Löwe, J (2006) Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol. Cell 23:457-69 |
|---|---|
| Abstract |
FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. We present crystal structures of the FtsK motor domain monomer, showing that it has a RecA-like core, the FtsK hexamer, and also showing that it is a ring with a large central annulus and a dodecamer consisting of two hexamers, head to head. Electron microscopy (EM) demonstrates the DNA-dependent existence of hexamers in solution and shows that duplex DNA passes through the middle of each ring. Comparison of FtsK monomer structures from two different crystal forms highlights a conformational change that we propose is the structural basis for a rotary inchworm mechanism of DNA translocation. |
| Links |
PubMed Online version:10.1016/j.molcel.2006.06.019 |
| Keywords |
Adenosine Triphosphate/metabolism; Crystallography, X-Ray; DNA Helicases/metabolism; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA, Bacterial/ultrastructure; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/ultrastructure; Hydrolysis; Integrases/metabolism; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Membrane Proteins/metabolism; Membrane Proteins/ultrastructure; Models, Genetic; Models, Molecular; Nucleic Acid Conformation; Pseudomonas aeruginosa/chemistry; RNA Helicases/metabolism; Rec A Recombinases/metabolism; Recombination, Genetic |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0033676: double-stranded DNA-dependent ATPase activity |
ECO:0000315: |
F |
As shown in figure 1C, wild type FtsK shows significant DNA-dependent ATPase activity in comparison to FtsK containing a mutation in the walker A motif, which sees significantly inhibited activity. |
complete | ||||
|
enables |
GO:0033676: double-stranded DNA-dependent ATPase activity |
ECO:0000315: mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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