9BE2

Structure of the E. coli nucleic associated protein, YejK

9BE2 の概要

• エントリーDOI: 10.2210/pdb9be2/pdb
• 分子名称: Nucleoid-associated protein YejK (1 entity in total)
• 機能のキーワード: nap, nucleoid associated protein, yejk, ndpa, dna binding clamp, non-sequence specific, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38145.66

構造登録者

Schumacher, M.A. (登録日: 2024-04-13, 公開日: 2024-05-15, 最終更新日: 2024-07-24)

主引用文献

Schumacher, M.A.,Singh, R.R.,Salinas, R.
Structure of the E. coli nucleoid-associated protein YejK reveals a novel DNA binding clamp.
Nucleic Acids Res., 52:7354-7366, 2024

PubMed Abstract: Nucleoid-associated proteins (NAPs) play central roles in bacterial chromosome organization and DNA processes. The Escherichia coli YejK protein is a highly abundant, yet poorly understood NAP. YejK proteins are conserved among Gram-negative bacteria but show no homology to any previously characterized DNA-binding protein. Hence, how YejK binds DNA is unknown. To gain insight into YejK structure and its DNA binding mechanism we performed biochemical and structural analyses on the E. coli YejK protein. Biochemical assays demonstrate that, unlike many NAPs, YejK does not show a preference for AT-rich DNA and binds non-sequence specifically. A crystal structure revealed YejK adopts a novel fold comprised of two domains. Strikingly, each of the domains harbors an extended arm that mediates dimerization, creating an asymmetric clamp with a 30 Å diameter pore. The lining of the pore is electropositive and mutagenesis combined with fluorescence polarization assays support DNA binding within the pore. Finally, our biochemical analyses on truncated YejK proteins suggest a mechanism for YejK clamp loading. Thus, these data reveal YejK contains a newly described DNA-binding motif that functions as a novel clamp.

PubMed: 38832628
DOI: 10.1093/nar/gkae459

実験手法

X-RAY DIFFRACTION (3.56 Å)