2MW2

Hha-H-NS46 charge zipper complex

2MW2 の概要

• エントリーDOI: 10.2210/pdb2mw2/pdb
• 関連するPDBエントリー: 1jw2 1NI8
• NMR情報: BMRB: 25296
• 分子名称: Hemolysin expression-modulating protein Hha, DNA-binding protein H-NS (2 entities in total)
• 機能のキーワード: nucleoid-associated proteins, charge-zipper complex, electrostatic-driven function, salt-dependent dynamics, dna binding protein
• 由来する生物種: Escherichia coli K-12; 詳細
• 細胞内の位置: Cytoplasm, nucleoid : P0ACF8
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 19576.48

構造登録者

Cordeiro, T.N.,Garcia, J.,Bernado, P.,Millet, O.,Pons, M. (登録日: 2014-10-24, 公開日: 2015-07-29, 最終更新日: 2024-05-01)

主引用文献

Cordeiro, T.N.,Garcia, J.,Bernado, P.,Millet, O.,Pons, M.
A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing.
J. Biol. Chem., 290:21200-21212, 2015

PubMed Abstract: The Hha/YmoA nucleoid-associated proteins help selectively silence horizontally acquired genetic material, including pathogenicity and antibiotic resistance genes and their maintenance in the absence of selective pressure. Members of the Hha family contribute to gene silencing by binding to the N-terminal dimerization domain of H-NS and modifying its selectivity. Hha-like proteins and the H-NS N-terminal domain are unusually rich in charged residues, and their interaction is mostly electrostatic-driven but, nonetheless, highly selective. The NMR-based structural model of the complex between Hha/YmoA and the H-NS N-terminal dimerization domain reveals that the origin of the selectivity is the formation of a three-protein charge zipper with interdigitated complementary charged residues from Hha and the two units of the H-NS dimer. The free form of YmoA shows collective microsecond-millisecond dynamics that can by measured by NMR relaxation dispersion experiments and shows a linear dependence with the salt concentration. The number of residues sensing the collective dynamics and the population of the minor form increased in the presence of H-NS. Additionally, a single residue mutation in YmoA (D43N) abolished H-NS binding and the dynamics of the apo-form, suggesting the dynamics and binding are functionally related.

PubMed: 26085102
DOI: 10.1074/jbc.M114.630400

実験手法

SOLUTION NMR