6RYK

Crystal structure of the ParB-like protein PadC

6RYK の概要

• エントリーDOI: 10.2210/pdb6ryk/pdb
• 分子名称: ParB-like nuclease domain protein, MAGNESIUM ION, CYTIDINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: parabs, cytoskeleton, bactofilin, ctp, cell cycle
• 由来する生物種: Myxococcus xanthus DK 1622
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51622.17

構造登録者

Altegoer, F.,Bange, G. (登録日: 2019-06-10, 公開日: 2020-01-22, 最終更新日: 2024-05-15)

主引用文献

Osorio-Valeriano, M.,Altegoer, F.,Steinchen, W.,Urban, S.,Liu, Y.,Bange, G.,Thanbichler, M.
ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches.
Cell, 179:1512-1524.e15, 2019

PubMed Abstract: During cell division, newly replicated DNA is actively segregated to the daughter cells. In most bacteria, this process involves the DNA-binding protein ParB, which condenses the centromeric regions of sister DNA molecules into kinetochore-like structures that recruit the DNA partition ATPase ParA and the prokaroytic SMC/condensin complex. Here, we report the crystal structure of a ParB-like protein (PadC) that emerges to tightly bind the ribonucleotide CTP. The CTP-binding pocket of PadC is conserved in ParB and composed of signature motifs known to be essential for ParB function. We find that ParB indeed interacts with CTP and requires nucleotide binding for DNA condensation in vivo. We further show that CTP-binding modulates the affinity of ParB for centromeric parS sites, whereas parS recognition stimulates its CTPase activity. ParB proteins thus emerge as a new class of CTP-dependent molecular switches that act in concert with ATPases and GTPases to control fundamental cellular functions.

PubMed: 31835030
DOI: 10.1016/j.cell.2019.11.015

実験手法

X-RAY DIFFRACTION (1.7 Å)