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. 2015 Oct 10;43(18):9065–9075. doi: 10.1093/nar/gkv861

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© The Author(s) 2015. 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 1. — Crystal structure of mtPAP. (A) Diagram of mtPAP domains with their boundaries indicated by residue numbers. (B) Front and (C) top views of the mtPAP homodimer. The three mtPAP domains are colored as in (A). The dimension of the dimer is marked by a bracket. (D) Superposition of the NTD of mtPAP (dotted circle) and the RRM domain 4 (pink) of polypyrimidine tract-binding protein (PDB code: 4CQ1), with the secondary-structure elements of mtPAP numbered. (E) The mtPAP monomer with secondary-structure elements labeled. The active sites are highlighted by the three carboxylates, which are shown as red sticks. Blue sticks indicate the N472 residue implicated in SPAX4 (see main text). Loops discussed in the text are indicated.