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. 2017 Aug 29;7:9903. doi: 10.1038/s41598-017-10085-8

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Crystal structure of an Hfq-poly(A) complex reveals interaction via base stacking of the RNA rings. (a) Overall view of the E. coli Hfq72-A₁₈ crystal structure showing a sandwich-like dimeric assembly of two RNA-bound Hfq hexamers. The two Hfq rings (grey) comprise amino acids 1–72 and are arranged with their distal faces oriented towards each other; the RNA chains (dark red/yellow) are located at the center between the proteins and form interlocked base stacking interactions holding the assembly together. (b) Close-up of the RNA interactions showing the A-site and R-site bases docked deep into Hfq’s surface and the flipped-out N-site bases interacting via base stacking and electrostatic interactions (dashed lines).