2VE9

Xray structure of KOPS bound gamma domain of FtsK (P. aeruginosa)

Summary for 2VE9

• Entry DOI: 10.2210/pdb2ve9/pdb
• Related: 2IUT 2IUU 2J5O 2VE8
• Descriptor: DNA TRANSLOCASE FTSK, 5'-D(*AP*CP*CP*AP*GP*GP*GP*CP*AP*GP *GP*GP*CP*GP*AP*C)-3', 5'-D(*GP*TP*CP*GP*CP*CP*CP*TP*GP*CP *CP*CP*TP*GP*GP*T)-3', ... (5 entities in total)
• Functional Keywords: nucleotide-binding, chromosome partition, atp-binding, dna-binding, translocase, winged helix, bacterial cell division, transport protein, cell division, transmembrane, inner membrane, ftsz, ftsk, membrane, cell cycle, dna binding
• Biological source: PSEUDOMONAS AERUGINOSA; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side: Q9I0M3
• Total number of polymer chains: 10
• Total formula weight: 67240.51

Authors

Lowe, J.,Allen, M.D.,Sherratt, D.J. (deposition date: 2007-10-17, release date: 2008-09-09, Last modification date: 2024-05-08)

Primary citation

Lowe, J.,Ellonen, A.,Allen, M.D.,Atkinson, C.,Sherratt, D.J.,Grainge, I.
Molecular Mechanism of Sequence-Directed DNA Loading and Translocation by Ftsk.
Mol.Cell, 31:498-, 2008

PubMed Abstract: Dimeric circular chromosomes, formed by recombination between monomer sisters, cannot be segregated to daughter cells at cell division. XerCD site-specific recombination at the Escherichia coli dif site converts these dimers to monomers in a reaction that requires the DNA translocase FtsK. Short DNA sequences, KOPS (GGGNAGGG), which are polarized toward dif in the chromosome, direct FtsK translocation. FtsK interacts with KOPS through a C-terminal winged helix domain gamma. The crystal structure of three FtsKgamma domains bound to 8 bp KOPS DNA demonstrates how three gamma domains recognize KOPS. Using covalently linked dimers of FtsK, we infer that three gamma domains per hexamer are sufficient to recognize KOPS and load FtsK and subsequently activate recombination at dif. During translocation, FtsK fails to recognize an inverted KOPS sequence. Therefore, we propose that KOPS act solely as a loading site for FtsK, resulting in a unidirectionally oriented hexameric motor upon DNA.

PubMed: 18722176
DOI: 10.1016/J.MOLCEL.2008.05.027

Experimental method

X-RAY DIFFRACTION (1.9 Å)