3KZ5
Structure of cdomain
Summary for 3KZ5
| Entry DOI | 10.2210/pdb3kz5/pdb |
| Descriptor | Protein sopB, ACETATE ION (3 entities in total) |
| Functional Keywords | partition, segregation, f plasmid, dna-binding protein, dna-binding, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 17467.28 |
| Authors | Schumacher, M.A. (deposition date: 2009-12-07, release date: 2010-03-31, Last modification date: 2024-02-21) |
| Primary citation | Schumacher, M.A.,Piro, K.M.,Xu, W. Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. Nucleic Acids Res., 38:4514-4526, 2010 Cited by PubMed Abstract: Accurate DNA segregation is essential for genome transmission. Segregation of the prototypical F plasmid requires the centromere-binding protein SopB, the NTPase SopA and the sopC centromere. SopB displays an intriguing range of DNA-binding properties essential for partition; it binds sopC to form a partition complex, which recruits SopA, and it also coats DNA to prevent non-specific SopA-DNA interactions, which inhibits SopA polymerization. To understand the myriad functions of SopB, we determined a series of SopB-DNA crystal structures. SopB does not distort its DNA site and our data suggest that SopB-sopC forms an extended rather than wrapped partition complex with the SopA-interacting domains aligned on one face. SopB is a multidomain protein, which like P1 ParB contains an all-helical DNA-binding domain that is flexibly attached to a compact (beta(3)-alpha)(2) dimer-domain. Unlike P1 ParB, the SopB dimer-domain does not bind DNA. Moreover, SopB contains a unique secondary dimerization motif that bridges between DNA duplexes. Both specific and non-specific SopB-DNA bridging structures were observed. This DNA-linking function suggests a novel mechanism for in trans DNA spreading by SopB, explaining how it might mask DNA to prevent DNA-mediated inhibition of SopA polymerization. PubMed: 20236989DOI: 10.1093/nar/gkq161 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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