3QHS

Crystal structure of full-length Hfq from Escherichia coli

3QHS の概要

• エントリーDOI: 10.2210/pdb3qhs/pdb
• 関連するPDBエントリー: 3QO3
• 分子名称: Protein hfq (2 entities in total)
• 機能のキーワード: rna binding protein, sm-like, pleiotropic regulator
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 134152.25

構造登録者

Beich-Frandsen, M.,Vecerek, B.,Sjoeblom, B.,Blaesi, U.,Djinovic-Carugo, K. (登録日: 2011-01-26, 公開日: 2011-05-18, 最終更新日: 2023-11-01)

主引用文献

Beich-Frandsen, M.,Vecerek, B.,Sjoblom, B.,Blasi, U.,Djinovic-Carugo, K.
Structural analysis of full-length Hfq from Escherichia coli
Acta Crystallogr.,Sect.F, 67:536-540, 2011

PubMed Abstract: The structure of full-length host factor Qβ (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 Å, α = 78.6, β = 86.2, γ = 59.9°, was solved by molecular replacement to a resolution of 2.85 Å and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover ~65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli.

PubMed: 21543856
DOI: 10.1107/S174430911100786X

実験手法

X-RAY DIFFRACTION (2.85 Å)