2JQT

Structure of the bacterial replication origin-associated protein Cnu

2JQT の概要

• エントリーDOI: 10.2210/pdb2jqt/pdb
• 関連するPDBエントリー: 1jw2
• 分子名称: H-NS/stpA-binding protein 2 (1 entity in total)
• 機能のキーワード: cnu, ydgt, replication origin associated, oric, h-ns, protein binding
• 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: 8428.57

構造登録者

Bae, S.H.,Liu, D.,Lim, H.M.,Lee, Y.,Choi, B.S. (登録日: 2007-06-07, 公開日: 2008-04-22, 最終更新日: 2023-12-20)

主引用文献

Bae, S.H.,Liu, D.,Lim, H.M.,Lee, Y.,Choi, B.S.
Structure of the nucleoid-associated protein Cnu reveals common binding sites for H-NS in Cnu and Hha.
Biochemistry, 47:1993-2001, 2008

PubMed Abstract: Cnu is a nucleoid protein that has a high degree of sequence homology with Hha/YmoA family proteins, which bind to chromatin and regulate the expression of Escherichia coli virulence genes in response to changes in temperature or ionic strength. Here, we determined its solution structure and dynamic properties and mapped H-NS binding sites. Cnu consists of three alpha helices that are comparable with those of Hha, but it has significant flexibility in the C-terminal region and lacks a short alpha helix present in Hha. Upon increasing ionic strength, the helical structure of Cnu is destabilized, especially at the ends of the helices. The dominant H-NS binding sites, located at helix 3 as in Hha, reveal a common structural platform for H-NS binding. Our results may provide structural and dynamic bases for the similarity and dissimilarity between Cnu and Hha functions.

PubMed: 18189420
DOI: 10.1021/bi701914t

実験手法

SOLUTION NMR