Abstract
FtsK is aDNA 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 rapidly and directionally, and reverse direction. We present crystal structures of the FtsK motor domain monomer, showing it has a RecA-like core, and the Ftsk hexamer, showing it is a ringwith a large central annulus. Electron microscopy 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. We also show that two hexamers of FtsK can form a head-to-head double-ring, which suggests a model for bidirectional DNA translocation by this protein. m06.o03
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