Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 May 16;18:7. doi: 10.1186/s12858-017-0084-2

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s). 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

PMC Copyright notice

Fig. 9 — Domain arrangement of PNK/CPDase proteins. a Multiple sequence alignment using T-Coffee [54]. Aligned sequences of ScTrl1 PNK/CPDase (Sc), BfPNK/CPDase (Bf), MmCNPase (mouse), and HsCNPase (human). The N-terminal P-loop motif and two C-terminal H-x-(T/S)-x motifs are underlined in red and green, respectively. b Superposition of the homology model of the CPDase domain of BfPNK/CPDase (blue), generated using Phyre ², and the crystal structure of the catalytic domain of MmCNPase (yellow) [PDB ID: 2YDB] [27, 53]. The black arrows point to the locations of flexible loops in the homology model of the CPDase domain of BfPNK/CPDase (blue). c The overall three-dimensional shapes of PNK/CPDase proteins determined in this study can be used to propose a structural arrangement of the domains