3KZ5

Structure of cdomain

3KZ5 の概要

• エントリーDOI: 10.2210/pdb3kz5/pdb
• 分子名称: Protein sopB, ACETATE ION (3 entities in total)
• 機能のキーワード: partition, segregation, f plasmid, dna-binding protein, dna-binding, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 17467.28

構造登録者

Schumacher, M.A. (登録日: 2009-12-07, 公開日: 2010-03-31, 最終更新日: 2024-02-21)

主引用文献

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

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: 20236989
DOI: 10.1093/nar/gkq161

実験手法

X-RAY DIFFRACTION (1.58 Å)