Journal
MOLECULAR CELL
Volume 23, Issue 4, Pages 457-469Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2006.06.019
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Funding
- Medical Research Council [MC_U105184326] Funding Source: Medline
- Wellcome Trust [GR068713MA, 068713] Funding Source: Medline
- MRC [MC_U105184326] Funding Source: UKRI
- Medical Research Council [MC_U105184326] Funding Source: researchfish
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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.
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