2J5P
E. coli FtsK gamma domain
Summary for 2J5P
Entry DOI | 10.2210/pdb2j5p/pdb |
Related | 2IUS 2J5O |
Descriptor | DNA TRANSLOCASE FTSK (1 entity in total) |
Functional Keywords | ftsk, kops, xercd, recombination, dna segregation, bacterial cell division |
Biological source | ESCHERICHIA COLI |
Cellular location | Cell inner membrane ; Multi-pass membrane protein : P46889 |
Total number of polymer chains | 1 |
Total formula weight | 8680.66 |
Authors | Sivanathan, V.,Allen, M.D.,de Bekker, C.,Baker, R.,Arciszewska, L.,Freund, S.M.,Bycroft, M.,Lowe, J.,Sherratt, D.J. (deposition date: 2006-09-19, release date: 2006-10-04, Last modification date: 2024-05-15) |
Primary citation | Sivanathan, V.,Allen, M.D.,De Bekker, C.,Baker, R.,Arciszewska, L.,Freund, S.M.,Bycroft, M.,Lowe, J.,Sherratt, D.J. The Ftsk Gamma Domain Directs Oriented DNA Translocation by Interacting with Kops. Nat.Struct.Mol.Biol., 13:965-, 2006 Cited by PubMed Abstract: The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating completion of chromosome segregation. Translocase functions reside in three domains, alpha, beta and gamma. FtsKalphabeta are necessary and sufficient for ATP hydrolysis-dependent DNA translocation, which is modulated by FtsKgamma through its interaction with KOPS. By solving the FtsKgamma structure by NMR, we show that gamma is a winged-helix domain. NMR chemical shift mapping localizes the DNA-binding site on the gamma domain. Mutated proteins with substitutions in the FtsKgamma DNA-recognition helix are impaired in DNA binding and KOPS recognition, yet remain competent in DNA translocation and XerCD-dif site-specific recombination, which facilitates the late stages of chromosome segregation. PubMed: 17057717DOI: 10.1038/NSMB1158 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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