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. 2014 Apr 5;42(10):6673–6685. doi: 10.1093/nar/gku249

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© The Author(s) 2014. 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/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Structure of the ThiI_Tm–RNA complex. (A) Ribbon representation of the ThiI_Tm monomer consisting of a NFLD (yellow), a THUMP domain (red) and a pyrophosphatase (PPase) domain (blue). (B) Ribbon representation of the ThiI homo-dimer. The dimerization interface is mainly formed by the PPase domains. (C) The ThiI_Tm homo-dimer binds two RNA molecules. The THUMP domain and the NFLD bind the acceptor stem, thereby positioning the U8 (position indicated by an arrow) close to the active site of the PPase domain of the other monomer. (D) View perpendicular to (C), showing how the three domains belonging to both monomers wrap around the RNA.