2IUU

P. aeruginosa FtsK motor domain, hexamer

Summary for 2IUU

• Entry DOI: 10.2210/pdb2iuu/pdb
• Related: 2IUS 2IUT
• Descriptor: DNA TRANSLOCASE FTSK, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: dna translocation, nucleotide-binding, atp-binding, dna-binding, cell division, transmembrane, chromosome partition, inner membrane, hexameric ring, membrane protein, kops, membrane, divisome, cell cycle, aaa atpase
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 6
• Total formula weight: 326571.85

Authors

Massey, T.H.,Mercogliano, C.P.,Yates, J.,Sherratt, D.J.,Lowe, J. (deposition date: 2006-06-07, release date: 2006-08-29, Last modification date: 2024-05-08)

Primary citation

Massey, T.H.,Mercogliano, C.P.,Yates, J.,Sherratt, D.J.,Lowe, J.
Double-Stranded DNA Translocation: Structure and Mechanism of Hexameric Ftsk
Mol.Cell, 23:457-, 2006

PubMed Abstract: 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.

PubMed: 16916635
DOI: 10.1016/J.MOLCEL.2006.06.019

Experimental method

X-RAY DIFFRACTION (2.9 Å)