Structural Studies of a Bacterial Condensin Complex Reveal ATP-Dependent Disruption of Intersubunit Interactions

Jae Sung Woo, Jae Hong Lim, Ho Chul Shin, Min Kang Suh, Bonsu Ku, Kwang Hoon Lee, Keehyoung Joo, Howard Robinson, Jooyoung Lee, Sam Yong Park, Nam Chul Ha, Byung Ha Oh

Research output: Contribution to journalArticlepeer-review

119 Citations (Scopus)


Condensins are key mediators of chromosome condensation across organisms. Like other condensins, the bacterial MukBEF condensin complex consists of an SMC family protein dimer containing two ATPase head domains, MukB, and two interacting subunits, MukE and MukF. We report complete structural views of the intersubunit interactions of this condensin along with ensuing studies that reveal a role for the ATPase activity of MukB. MukE and MukF together form an elongated dimeric frame, and MukF's C-terminal winged-helix domains (C-WHDs) bind MukB heads to constitute closed ring-like structures. Surprisingly, one of the two bound C-WHDs is forced to detach upon ATP-mediated engagement of MukB heads. This detachment reaction depends on the linker segment preceding the C-WHD, and mutations on the linker restrict cell growth. Thus ATP-dependent transient disruption of the MukB-MukF interaction, which creates openings in condensin ring structures, is likely to be a critical feature of the functional mechanism of condensins.

Original languageEnglish
Pages (from-to)85-96
Number of pages12
Issue number1
Publication statusPublished - 2009 Jan 9
Externally publishedYes



ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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