6OZX

Wild type GapR crystal structure 1 from C. crescentus

6OZX の概要

• エントリーDOI: 10.2210/pdb6ozx/pdb
• 分子名称: UPF0335 protein CC_3319 (2 entities in total)
• 機能のキーワード: dna-binding, cell-division, dna binding protein
• 由来する生物種: Caulobacter vibrioides (strain ATCC 19089 / CB15)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12911.60

構造登録者

Tarry, M.,Harmel, C.,Taylor, J.A.,Marczynski, G.T.,Schmeing, T.M. (登録日: 2019-05-16, 公開日: 2019-11-27, 最終更新日: 2024-03-13)

主引用文献

Tarry, M.J.,Harmel, C.,Taylor, J.A.,Marczynski, G.T.,Schmeing, T.M.
Structures of GapR reveal a central channel which could accommodate B-DNA.
Sci Rep, 9:16679-16679, 2019

PubMed Abstract: GapR is a nucleoid-associated protein required for the cell cycle of Caulobacter cresentus. We have determined new crystal structures of GapR to high resolution. As in a recently published structure, a GapR monomer folds into one long N-terminal α helix and two shorter α helices, and assembles into a tetrameric ring with a closed, positively charged, central channel. In contrast to the conclusions drawn from the published structures, we observe that the central channel of the tetramer presented here could freely accommodate B-DNA. Mutation of six conserved lysine residues lining the cavity and electrophoretic mobility gel shift experiments confirmed their role in DNA binding and the channel as the site of DNA binding. Although present in our crystals, DNA could not be observed in the electron density maps, suggesting that DNA binding is non-specific, which could be important for tetramer-ring translocation along the chromosome. In conjunction with previous GapR structures we propose a model for DNA binding and translocation that explains key published observations on GapR and its biological functions.

PubMed: 31723182
DOI: 10.1038/s41598-019-52964-2

実験手法

X-RAY DIFFRACTION (1.851 Å)