7BNR

Crystal structure of a ParB Q52A mutant from Myxococcus xanthus bound to CTPyS

7BNR の概要

• エントリーDOI: 10.2210/pdb7bnr/pdb
• 分子名称: ParB family protein, Cytosine 5'-[gamma-thio]triphosphate, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: dna-binding protein, ctp, myxococcus, dna-segregation, dna binding protein
• 由来する生物種: Myxococcus xanthus (strain DK 1622)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48010.96

構造登録者

Altegoer, F.,Bange, G. (登録日: 2021-01-22, 公開日: 2021-09-08, 最終更新日: 2024-01-31)

主引用文献

Osorio-Valeriano, M.,Altegoer, F.,Das, C.K.,Steinchen, W.,Panis, G.,Connolley, L.,Giacomelli, G.,Feddersen, H.,Corrales-Guerrero, L.,Giammarinaro, P.I.,Hanssmann, J.,Bramkamp, M.,Viollier, P.H.,Murray, S.,Schafer, L.V.,Bange, G.,Thanbichler, M.
The CTPase activity of ParB determines the size and dynamics of prokaryotic DNA partition complexes.
Mol.Cell, 81:3992-, 2021

PubMed Abstract: ParB-like CTPases mediate the segregation of bacterial chromosomes and low-copy number plasmids. They act as DNA-sliding clamps that are loaded at parS motifs in the centromere of target DNA molecules and spread laterally to form large nucleoprotein complexes serving as docking points for the DNA segregation machinery. Here, we solve crystal structures of ParB in the pre- and post-hydrolysis state and illuminate the catalytic mechanism of nucleotide hydrolysis. Moreover, we identify conformational changes that underlie the CTP- and parS-dependent closure of ParB clamps. The study of CTPase-deficient ParB variants reveals that CTP hydrolysis serves to limit the sliding time of ParB clamps and thus drives the establishment of a well-defined ParB diffusion gradient across the centromere whose dynamics are critical for DNA segregation. These findings clarify the role of the ParB CTPase cycle in partition complex assembly and function and thus advance our understanding of this prototypic CTP-dependent molecular switch.

PubMed: 34562373
DOI: 10.1016/j.molcel.2021.09.004

実験手法

X-RAY DIFFRACTION (1.7 Å)