Sequence and structural alignment of Nu class GSTs with a Sigma Class GST (HsGST, human GST or hematopoietic prostagladin D synthase 37) and other parasite GSTs (SjGST, 43, (-GST-1) 42

<p><b>Copyright information:</b></p><p>Taken from "X-ray structures of -GST-1 and -GST-2 two glutathione s-transferase from the human hookworm "</p><p>http://www.biomedcentral.com/1472-6807/7/42</p><p>BMC Structural Biology 2007;7():42-42.</p><p>Published online 26 Jun 2007</p><p>PMCID:PMC1924862.</p><p></p> (a) The alignment reveals that firstly N-terminal alpha beta domain is more conserved than the C-terminal alpha domain. Furthermore, -GST-1 has higher sequence identity with HpolGST than -GST-2 and the lowest similarity is with the HsGST. This figure was generated with ESPript [55, 56]. (b) Structural alignment of monomers of Nu class GSTs (-GST-1, magenta; -GST-2, gold; HpolGST, green) with a sigma class GST (HsGST, cyan)

Nu class GSTs a) -GST-2, c) HpolGST have larger binding cavity than sigma class GST b) HsGST

<p><b>Copyright information:</b></p><p>Taken from "X-ray structures of -GST-1 and -GST-2 two glutathione s-transferase from the human hookworm "</p><p>http://www.biomedcentral.com/1472-6807/7/42</p><p>BMC Structural Biology 2007;7():42-42.</p><p>Published online 26 Jun 2007</p><p>PMCID:PMC1924862.</p><p></p> d) Overlay of the cavities reveals the considerable reduction in the active site size between sigma class (blue) and nu class (cyan). The structure of HpolGST is missing a loop in close proximity to the binding cavity and we modeled it as cartoon from the -GST-2 structure. The glutathione in the G-site is shown as red stick model