posted on 2017-12-19, 05:00authored byAnkit Dwivedi, Christelle Reynes, Axel Kuehn, Daniel Roche, Nimol Khim, Maxim Hebrard, Sylvain Milanesi, Eric Rivals, Roger Frutos, Didier Menard, Choukri Mamoun, Jacques Colinge, Emmanuel Cornillot
Additional file 15. Structural comparison of 30S ribosomal protein S10 protein models from Neisseria gonorrhoeae, Neisseria meningitidis and Plasmodium falciparum, which can mediate tetracycline resistance. a Model of the N. gonorrhoeae 30S ribosomal S10 protein (NCBI GI#501495768), colored in blue. b Model of the N. meningitidis 30S ribosomal S10 protein (NCBI GI#488148952), in green. c Model of the P. falciparum PF3D7_1460900.1 protein, with the central domain colored in red, with two N-terminal (residues 1–68) and C-terminal (residues 180–274) domains colored grey. d Model of the P. falciparum PF3D7_1460900.2 protein, with the central domain colored in forest green, with two N-terminal (residues 1–68) and C-terminal (residues 176-268) domains colored grey. e Shows the superposition of a (blue) and c (red), with a TM-score of 0.8549. f Shows the superposition of a (blue) and d (forest green), with a TM-score of 0.8736. g Shows the superposition of b (green) and c (red), with a TM-score of 0.8610. h Shows the superposition of b (green) and d (forest green), with a TM-score of 0.8786. Proteins models were constructed using the RaptorX server [40]. TM-score and protein superposition determined using TM-align [43]. TM-scores above 0.5 indicate the proteins have the same fold. All images were rendered in PyMOL. A zoom in the loop containing the putative tetracycline resistance mutation is inserted in e–h panels.