7DUT

Structure of Sulfolobus solfataricus SegA protein

7DUT の概要

• エントリーDOI: 10.2210/pdb7dut/pdb
• 分子名称: SOJ protein (Soj), ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: partition protein, dna binding protein
• 由来する生物種: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24775.85

構造登録者

Yen, C.Y.,Lin, M.G.,Hsiao, C.D.,Sun, Y.J. (登録日: 2021-01-11, 公開日: 2021-12-22, 最終更新日: 2023-11-29)

主引用文献

Yen, C.Y.,Lin, M.G.,Chen, B.W.,Ng, I.W.,Read, N.,Kabli, A.F.,Wu, C.T.,Shen, Y.Y.,Chen, C.H.,Barilla, D.,Sun, Y.J.,Hsiao, C.D.
Chromosome segregation in Archaea: SegA- and SegB-DNA complex structures provide insights into segrosome assembly.
Nucleic Acids Res., 49:13150-13164, 2021

PubMed Abstract: Genome segregation is a vital process in all organisms. Chromosome partitioning remains obscure in Archaea, the third domain of life. Here, we investigated the SegAB system from Sulfolobus solfataricus. SegA is a ParA Walker-type ATPase and SegB is a site-specific DNA-binding protein. We determined the structures of both proteins and those of SegA-DNA and SegB-DNA complexes. The SegA structure revealed an atypical, novel non-sandwich dimer that binds DNA either in the presence or in the absence of ATP. The SegB structure disclosed a ribbon-helix-helix motif through which the protein binds DNA site specifically. The association of multiple interacting SegB dimers with the DNA results in a higher order chromatin-like structure. The unstructured SegB N-terminus plays an essential catalytic role in stimulating SegA ATPase activity and an architectural regulatory role in segrosome (SegA-SegB-DNA) formation. Electron microscopy results also provide a compact ring-like segrosome structure related to chromosome organization. These findings contribute a novel mechanistic perspective on archaeal chromosome segregation.

PubMed: 34850144
DOI: 10.1093/nar/gkab1155

実験手法

X-RAY DIFFRACTION (2.1 Å)