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. 2020 Dec;26(12):2031–2043. doi: 10.1261/rna.077354.120

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© 2020 Immer et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 5. — Lpp1663 interacts with RNA through its core domain and mainly with the concave face of the protein. (A) Sections of ¹H, ¹⁵N HSQC spectra of ¹⁵N-labeled Lpp1663 titrated with oligo U₆, A₆, C₆, or a G-rich hexameric RNA. NMR signal assignments are given for residues undergoing substantial changes in signal intensity or chemical shift in the oligo U₆ titration. (B) Results of the NMR-titrations (three equivalents of RNA) were plotted on the surface of one of the lowest energy structures of Lpp1663. Changes in the chemical shift are indicated as the following: (red) peak disappeared, (blue) small shift, (gray) no change, (black) unclear. The most affected region is the concave face of Lp1663 as can be seen for oligo U₆ and oligo A₆. For oligo C₆ and the G-rich RNA, mostly minor chemical shift changes can be observed. The amino- and carboxyl termini are not involved in RNA-binding. Amino- and carboxyl termini are indicated as N and C, respectively.