Structural analysis of full-length Hfq from Escherichia coli

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-05, Vol.67 (5), p.536-540
• Main Authors: Beich-Frandsen, Mads, Vecerek, Branislav, Sjoblom, Bjorn, Blaesi, Udo, Djinovic-Carugo, Kristina
• Format: Article
• Language: English
• Subjects: Amino acids; crystal packing; Crystallization; Crystallography, X-Ray; E coli; Escherichia coli; Escherichia coli - chemistry; Escherichia coli Proteins - chemistry; Hfq; Host Factor 1 Protein - chemistry; Models, Molecular; Protein Structure, Quaternary; riboregulation; RNA chaperones; Structural analysis; Structural Communications
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S174430911100786X

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 Rwork and Rfree 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.