2ius | pdb_00002ius
E. COLI FTSK MOTOR DOMAIN
Overview
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 Structure
2IUS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 07:54:39 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
- Kop
- Membrane
- Membrane protein
- Nucleotide-binding
- Transmembrane
