9EFE

Crystal Structure in space group P21 of a nucleoid-associated protein (UBP) from Sulfolobus islandicus.

9EFE の概要

• エントリーDOI: 10.2210/pdb9efe/pdb
• 分子名称: Plasmid pARN4, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: sulfolobus islandicus, archaea, dna sequence specific binding protein, nucleoid-associated protein, dna replication origin binding protein, dna binding protein
• 由来する生物種: Sulfolobus islandicus REY15A
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 110584.79

構造登録者

Dhanaraju, R.,Gonzalez-Gutierrez, G.,Bell, S.D. (登録日: 2024-11-20, 公開日: 2025-06-11, 最終更新日: 2025-06-18)

主引用文献

Dhanaraju, R.,Samson, R.Y.,Feng, X.,Costa, A.,Gonzalez-Gutierrez, G.,Bell, S.D.
An archaeal nucleoid-associated protein binds an essential motif in DNA replication origins.
Nat Commun, 16:5230-5230, 2025

PubMed Abstract: DNA replication typically has defined start sites, or replication origins, which are designated by their recognition by specific initiator proteins. In addition to initiators, general chromatin or nucleoid-associated proteins have been shown to play roles in modulating origin efficiency in eukaryotes and bacteria. The role of chromatin proteins in origin function in the archaeal domain of life is poorly understood. Here, we describe a dissection of sequences elements required for in vivo function of an archaeal DNA replication origin. Our data reveal a hitherto uncharacterized sequence element, the ucm, is required for origin activity. We identify a protein, UBP, that interacts with the ucm and additionally with hundreds of other sites on the genome. We solve the crystal structure of UBP alone and in complex with ucm DNA, and further show that UBP interacts with the MCM replicative helicase. Taken together, our data provide evidence that UBP functions as a general nucleoid-associated protein that plays a key role in facilitating the egress of the MCM replicative helicase from DNA replication origins.

PubMed: 40473630
DOI: 10.1038/s41467-025-60618-3

実験手法

X-RAY DIFFRACTION (2.59 Å)