3M4G

H57A HFQ from Pseudomonas Aeruginosa

3M4G の概要

• エントリーDOI: 10.2210/pdb3m4g/pdb
• 関連するPDBエントリー: 1U1S 1U1T 3INZ
• 分子名称: Protein hfq, ZINC ION (3 entities in total)
• 機能のキーワード: hfq, protein tertiary structure, rna-binding, protein stability, stress response, rna binding protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 109484.74

構造登録者

Moskaleva, O.,Melnik, B.,Gabdulkhakov, A.,Garber, M.,Nikonov, S.,Stolboushkina, E.,Nikulin, A. (登録日: 2010-03-11, 公開日: 2010-07-28, 最終更新日: 2023-09-06)

主引用文献

Moskaleva, O.,Melnik, B.,Gabdulkhakov, A.,Garber, M.,Nikonov, S.,Stolboushkina, E.,Nikulin, A.
The structures of mutant forms of Hfq from Pseudomonas aeruginosa reveal the importance of the conserved His57 for the protein hexamer organization.
Acta Crystallogr.,Sect.F, 66:760-764, 2010

PubMed Abstract: The bacterial Sm-like protein Hfq forms homohexamers both in solution and in crystals. The monomers are organized as a continuous beta-sheet passing through the whole hexamer ring with a common hydrophobic core. Analysis of the Pseudomonas aeruginosa Hfq (PaeHfq) hexamer structure suggested that solvent-inaccessible intermonomer hydrogen bonds created by conserved amino-acid residues should also stabilize the quaternary structure of the protein. In this work, one such conserved residue, His57, in PaeHfq was replaced by alanine, threonine or asparagine. The crystal structures of His57Thr and His57Ala Hfq were determined and the stabilities of all of the mutant forms and of the wild-type protein were measured. The results obtained demonstrate the great importance of solvent-inaccessible conserved hydrogen bonds between the Hfq monomers in stabilization of the hexamer structure.

PubMed: 20606268
DOI: 10.1107/S1744309110017331

実験手法

X-RAY DIFFRACTION (2.05 Å)