3EUH
Crystal Structure of the MukE-MukF Complex
3EUH の概要
| エントリーDOI | 10.2210/pdb3euh/pdb |
| 関連するPDBエントリー | 3EUJ 3EUK |
| 分子名称 | Chromosome partition protein mukF, MukE, GLYCINE, ... (4 entities in total) |
| 機能のキーワード | chromosome condensation, condensin, non-smc subunit, kleisin, muke, mukf, calcium, cell cycle, cell division, chromosome partition, cytoplasm, dna condensation |
| 由来する生物種 | Escherichia coli 詳細 |
| 細胞内の位置 | Cytoplasm, nucleoid: P60293 Q6ITT5 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 209597.66 |
| 構造登録者 | |
| 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 Cited by 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: 19135891DOI: 10.1016/j.cell.2008.10.050 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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