8FVX

Histone from Bdellovibrio bacteriovorus

8FVX の概要

• エントリーDOI: 10.2210/pdb8fvx/pdb
• 分子名称: CBFD_NFYB_HMF domain-containing protein (2 entities in total)
• 機能のキーワード: histone, nap, dna binding protein
• 由来する生物種: Bdellovibrio bacteriovorus HD100
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6994.31

構造登録者

Laursen, S.P.,Luger, K. (登録日: 2023-01-19, 公開日: 2023-08-30, 最終更新日: 2024-03-13)

主引用文献

Hocher, A.,Laursen, S.P.,Radford, P.,Tyson, J.,Lambert, C.,Stevens, K.M.,Montoya, A.,Shliaha, P.V.,Picardeau, M.,Sockett, R.E.,Luger, K.,Warnecke, T.
Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus.
Nat Microbiol, 8:2006-2019, 2023

PubMed Abstract: Histone proteins bind DNA and organize the genomes of eukaryotes and most archaea, whereas bacteria rely on different nucleoid-associated proteins. Homology searches have detected putative histone-fold domains in a few bacteria, but whether these function like archaeal/eukaryotic histones is unknown. Here we report that histones are major chromatin components in the bacteria Bdellovibrio bacteriovorus and Leptospira interrogans. Patterns of sequence evolution suggest important roles for histones in additional bacterial clades. Crystal structures (<2.0 Å) of the B. bacteriovorus histone (Bd0055) dimer and the histone-DNA complex confirm conserved histone-fold topology but indicate a distinct DNA-binding mode. Unlike known histones in eukaryotes, archaea and viruses, Bd0055 binds DNA end-on, forming a sheath of dimers encasing straight DNA rather than wrapping DNA around their outer surface. Our results demonstrate that histones are present across the tree of life and highlight potential evolutionary innovation in how they associate with DNA.

PubMed: 37814071
DOI: 10.1038/s41564-023-01492-x

実験手法

X-RAY DIFFRACTION (1.8 Å)