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. 2014 May 13;460(Pt 2):199–210. doi: 10.1042/BJ20131540

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© 2014 The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Licence (CC-BY)(http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

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The conserved FAD-binding catalytic domain (black) contains a redox-active CXXC disulfide and a structural CX₁₆C disulfide. An additional shuttle disulfide is located at non-conserved domain (white). The architecture of LtErv is slightly altered with a KISS (Kinetoplastida-specific second) domain (grey) of approximately ~200 amino acids at the C-terminus. Hs, Homo sapiens; Sc, S. cerevisiae.