5XEI

Crystal structure of the Smc head domain with a coiled coil and joint derived from Pyrococcus yayanosii

5XEI の概要

• エントリーDOI: 10.2210/pdb5xei/pdb
• 分子名称: Chromosome partition protein Smc (2 entities in total)
• 機能のキーワード: condensin, smc, head domain, abc-atpase, dna binding protein, cell cycle
• 由来する生物種: Pyrococcus yayanosii (strain CH1 / JCM 16557); 詳細
• 細胞内の位置: Cytoplasm : F8AFS8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60825.11

構造登録者

Lee, H.,Noh, H.,Oh, B.-H. (登録日: 2017-04-05, 公開日: 2017-06-07, 最終更新日: 2023-11-22)

主引用文献

Diebold-Durand, M.L.,Lee, H.,Ruiz Avila, L.B.,Noh, H.,Shin, H.C.,Im, H.,Bock, F.P.,Burmann, F.,Durand, A.,Basfeld, A.,Ham, S.,Basquin, J.,Oh, B.-H.,Gruber, S.
Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization
Mol. Cell, 67:334-347.e5, 2017

PubMed Abstract: Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double helices. SMC subunits comprise an ABC ATPase "head" and a "hinge" dimerization domain connected by a 49 nm coiled-coil "arm." The heads undergo ATP-dependent engagement and disengagement to drive SMC action on the chromosome. Here, we elucidate the architecture of prokaryotic Smc dimers by high-throughput cysteine cross-linking and crystallography. Co-alignment of the Smc arms tightly closes the interarm space and misaligns the Smc head domains at the end of the rod by close apposition of their ABC signature motifs. Sandwiching of ATP molecules between Smc heads requires them to substantially tilt and translate relative to each other, thereby opening up the Smc arms. We show that this mechanochemical gating reaction regulates chromosome targeting and propose a mechanism for DNA translocation based on the merging of DNA loops upon closure of Smc arms.

PubMed: 28689660
DOI: 10.1016/j.molcel.2017.06.010

実験手法

X-RAY DIFFRACTION (2.599 Å)