3EUH

Crystal Structure of the MukE-MukF Complex

Summary for 3EUH

• Entry DOI: 10.2210/pdb3euh/pdb
• Related: 3EUJ 3EUK
• Descriptor: Chromosome partition protein mukF, MukE, GLYCINE, ... (4 entities in total)
• Functional Keywords: chromosome condensation, condensin, non-smc subunit, kleisin, muke, mukf, calcium, cell cycle, cell division, chromosome partition, cytoplasm, dna condensation
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm, nucleoid: P60293 Q6ITT5
• Total number of polymer chains: 6
• Total formula weight: 209597.66

Authors

Suh, M.K.,Ku, B.,Ha, N.C.,Woo, J.S.,Oh, B.H. (deposition date: 2008-10-10, release date: 2009-01-20, Last modification date: 2023-12-27)

Primary citation

Woo, J.S.,Lim, J.H.,Shin, H.C.,Suh, M.K.,Ku, B.,Lee, K.H.,Joo, K.,Robinson, H.,Lee, J.,Park, S.Y.,Ha, N.C.,Oh, B.H.
Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions.
Cell(Cambridge,Mass.), 136:85-96, 2009

PubMed Abstract: 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.

PubMed: 19135891
DOI: 10.1016/j.cell.2008.10.050

Experimental method

X-RAY DIFFRACTION (2.9 Å)