7BM8

Crystal structure of the C-terminally truncated chromosome-partitioning protein ParB from Caulobacter crescentus complexed with CTP-gamma-S

7BM8 の概要

• エントリーDOI: 10.2210/pdb7bm8/pdb
• 関連するPDBエントリー: 6T1F
• 分子名称: Chromosome-partitioning protein ParB, CYTIDINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: chromosome segregation, ctp, molecular gates, protein-dna recognition, dna binding protein
• 由来する生物種: Caulobacter vibrioides (strain NA1000 / CB15N)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57064.64

構造登録者

Jalal, A.S.,Tran, N.T.,Stevenson, C.E.M.,Lawson, D.M.,Le, T.B.K. (登録日: 2021-01-19, 公開日: 2021-04-28, 最終更新日: 2024-01-31)

主引用文献

Jalal, A.S.,Tran, N.T.,Stevenson, C.E.,Chimthanawala, A.,Badrinarayanan, A.,Lawson, D.M.,Le, T.B.
A CTP-dependent gating mechanism enables ParB spreading on DNA.
Elife, 10:-, 2021

PubMed Abstract: Proper chromosome segregation is essential in all living organisms. The ParA-ParB- system is widely employed for chromosome segregation in bacteria. Previously, we showed that ParB requires cytidine triphosphate to escape the nucleation site and spread by sliding to the neighboring DNA (Jalal et al., 2020). Here, we provide the structural basis for this transition from nucleation to spreading by solving co-crystal structures of a C-terminal domain truncated ParB with and with a CTP analog. Nucleating ParB is an open clamp, in which is captured at the DNA-binding domain (the DNA-gate). Upon binding CTP, the N-terminal domain (NTD) self-dimerizes to close the NTD-gate of the clamp. The DNA-gate also closes, thus driving into a compartment between the DNA-gate and the C-terminal domain. CTP hydrolysis and/or the release of hydrolytic products are likely associated with reopening of the gates to release DNA and recycle ParB. Overall, we suggest a CTP-operated gating mechanism that regulates ParB nucleation, spreading, and recycling.

PubMed: 34397383
DOI: 10.7554/eLife.69676

実験手法

X-RAY DIFFRACTION (2.73 Å)