3EUK

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

3EUK の概要

• エントリーDOI: 10.2210/pdb3euk/pdb
• 関連するPDBエントリー: 3EUH 3EUJ
• 分子名称: Chromosome partition protein mukB, Linker, Chromosome partition protein mukF, Chromosome partition protein mukE, ... (5 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Haemophilus ducreyi (strain 35000HP / ATCC 700724); 詳細
• 細胞内の位置: Cytoplasm, nucleoid : Q7VL96 Q7VL94 Q7VL95
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 306901.48

構造登録者

Woo, J.S.,Lim, J.H.,Shin, H.C.,Oh, B.H. (登録日: 2008-10-10, 公開日: 2009-01-20, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (4 Å)