2010年5月
Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
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- 巻
- 66
- 号
- Part 5
- 開始ページ
- 563
- 終了ページ
- 566
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S1744309110009942
- 出版者・発行元
- WILEY-BLACKWELL PUBLISHING, INC
The Hfq protein is a hexameric RNA-binding protein which regulates gene expression by binding to RNA under the influence of diverse environmental stresses. Its ring structure binds various types of RNA, including mRNA and sRNA. RNA-bound structures of Hfq from Escherichia coli and Staphylococcus aureus have been revealed to have poly(A) RNA at the distal site and U-rich RNA at the proximal site, respectively. Here, crystals of a complex of the Bacillus subtilis Hfq protein with an A/G-repeat 7-mer RNA (Hfq-RNA) that were prepared using the hanging-drop vapour-diffusion technique are reported. The type 1 Hfq-RNA crystals belonged to space group I422, with unit-cell parameters a = b = 123.70, c = 119.13 angstrom, while the type 2 Hfq-RNA crystals belonged to space group F222, with unit-cell parameters a = 91.92, b = 92.50, c = 114.92 angstrom. Diffraction data were collected to a resolution of 2.20 angstrom from both crystal forms. The hexameric structure of the Hfq protein was clearly shown by self-rotation analysis.
- リンク情報
- ID情報
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- DOI : 10.1107/S1744309110009942
- ISSN : 1744-3091
- Web of Science ID : WOS:000277217700020