3EUJ

Crystal structure of MukE-MukF(residues 292-443)-MukB(head domain)-ATPgammaS complex, symmetric dimer

Summary for 3EUJ

• Entry DOI: 10.2210/pdb3euj/pdb
• Related: 3EUH 3EUK
• Descriptor: Chromosome partition protein mukB, Linker, Chromosome partition protein mukF, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: mukb, muke, mukf, chromosome condensation, condensin, smc, non-smc subunit, abc-type atpase, whd, atp-binding, cell cycle, cell division, chromosome partition, dna condensation, dna-binding, nucleotide-binding
• Biological source: Haemophilus ducreyi (strain 35000HP / ATCC 700724); More
• Cellular location: Cytoplasm, nucleoid : Q7VL96 Q7VL94
• Total number of polymer chains: 2
• Total formula weight: 71984.87

Authors

Woo, J.S.,Lim, J.H.,Shin, H.C.,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 (3.1 Å)