7NG0

Crystal structure of N- and C-terminally truncated Geobacillus thermoleovorans nucleoid occlusion protein Noc

7NG0 の概要

• エントリーDOI: 10.2210/pdb7ng0/pdb
• 分子名称: Nucleoid occlusion protein, SULFATE ION (2 entities in total)
• 機能のキーワード: ctp switch, chromosome segregation, protein-dna recognition, peripheral membrane protein, dna binding protein
• 由来する生物種: Geobacillus thermoleovorans CCB_US3_UF5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26489.82

構造登録者

Jalal, A.S.B.,Tran, N.T.,Wu, L.J.,Ramakrishnan, K.,Rejzek, M.,Stevenson, C.E.M.,Lawson, D.M.,Errington, J.,Le, T.B.K. (登録日: 2021-02-08, 公開日: 2021-02-17, 最終更新日: 2024-01-31)

主引用文献

Jalal, A.S.B.,Tran, N.T.,Wu, L.J.,Ramakrishnan, K.,Rejzek, M.,Gobbato, G.,Stevenson, C.E.M.,Lawson, D.M.,Errington, J.,Le, T.B.K.
CTP regulates membrane-binding activity of the nucleoid occlusion protein Noc.
Mol.Cell, 81:3623-3636.e6, 2021

PubMed Abstract: ATP- and GTP-dependent molecular switches are extensively used to control functions of proteins in a wide range of biological processes. However, CTP switches are rarely reported. Here, we report that a nucleoid occlusion protein Noc is a CTPase enzyme whose membrane-binding activity is directly regulated by a CTP switch. In Bacillus subtilis, Noc nucleates on 16 bp NBS sites before associating with neighboring non-specific DNA to form large membrane-associated nucleoprotein complexes to physically occlude assembly of the cell division machinery. By in vitro reconstitution, we show that (1) CTP is required for Noc to form the NBS-dependent nucleoprotein complex, and (2) CTP binding, but not hydrolysis, switches Noc to a membrane-active state. Overall, we suggest that CTP couples membrane-binding activity of Noc to nucleoprotein complex formation to ensure productive recruitment of DNA to the bacterial cell membrane for nucleoid occlusion activity.

PubMed: 34270916
DOI: 10.1016/j.molcel.2021.06.025

実験手法

X-RAY DIFFRACTION (2.95 Å)