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. 2019 Apr 12;47(10):5420–5428. doi: 10.1093/nar/gkz269

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© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Structural features of the WYL domain of RspWYL1. (A) Structural comparison of the WYL domain of RspWYL1 (orange) and BsHfq (gray)-RNA (pink) complex (PDB: 3HSB). (B) Four residues Phe24, Phe29, Asn30 and Arg32 in BsHfq are responsible for recognition of RNA. Arg32 in BsHfq plays a significant role in binding RNA. (C) ITC binding curves of the R219D/R221D mutant with ssRNA. (D) Electrostatic surface representations of BsHfq. (E) Electrostatic surface representations of the WYL domain of RspWYL1. The helical extension of WYL domain is positively charged.