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. 2014 Feb 25;15(2):R27. doi: 10.1186/gb-2014-15-2-r27

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Copyright © 2014 Riveron et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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.

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GSTe2 three-dimensional structure variations reveal that L119F is important for DDT resistance. (A) Overlay of Benin-GSTe2 (purple) and Uganda-GSTe2 (green) structures and a close-up of the H4/H8 helices containing the L119F mutation. (B) Overlay of Uganda-GSTe2 (green) and An. gambiae GSTe2 (grey) structures showing their very similar conformation. (C) Comparison of the substrate-binding pockets of Benin-GSTe2 (purple) and Uganda-GSTe2 (green). (Left) The molecular surface representation of the H-site shows that DDT docks well into the Benin-GSTe2 binding site but clashes with the Uganda-GSTe2 structure. (Right) Close-up of the effect of L119F on the H-site (this mutation bends H4, leading to an increase in the DDT-binding cavity in Benin-GSTe2 but not for Uganda-GSTe2). Ct, C-terminal; DDT, dichlorodiphenyltrichloroethane; GSH, glutathione; Nt, N-terminal.