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Crystal structure of YmaH (Hfq) from Bacillus subtilis in complex with an RNA aptamer.Crystal structure of YmaH (Hfq) from Bacillus subtilis in complex with an RNA aptamer.
Structural highlights
Publication Abstract from PubMedThe 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 A, 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 A. Diffraction data were collected to a resolution of 2.20 A from both crystal forms. The hexameric structure of the Hfq protein was clearly shown by self-rotation analysis. Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer.,Baba S, Someya T, Kawai G, Nakamura K, Kumasaka T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt, 5):563-6. Epub 2010 Apr 30. PMID:20445260[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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