2iut
From Proteopedia
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P. AERUGINOSA FTSK MOTOR DOMAIN, DIMERIC
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
2IUT is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Known structural/functional Site: . 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 Thu Feb 21 17:56:13 2008
Categories: Pseudomonas aeruginosa | Single protein | Lowe, J. | Massey, T H. | Mercogliano, C P. | Sherratt, D J. | Yates, J. | ATG | MG | 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
