2ius
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E. COLI FTSK MOTOR DOMAIN
OverviewOverview
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.
About this StructureAbout this Structure
2IUS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Double-stranded DNA translocation: structure and mechanism of hexameric FtsK., Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J, Mol Cell. 2006 Aug;23(4):457-69. PMID:16916635
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- Escherichia coli
- Single protein
- Lowe, J.
- Massey, T.H.
- Mercogliano, C.P.
- Sherratt, D.J.
- Yates, J.
- Aaa atpase
- Atp-binding
- Cell cycle
- Cell division
- Chromosome partition
- Divisome
- Dna translocation
- Dna-binding
- Hexameric ring
- Inner membrane
- Kops
- Membrane
- Membrane protein
- Nucleotide-binding
- Transmembrane