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Figure 1 | BMC Structural Biology

Figure 1

From: An unexpected phosphate binding site in Glyceraldehyde 3-Phosphate Dehydrogenase: Crystal structures of apo, holo and ternary complex of Cryptosporidium parvum enzyme

Figure 1

Cofactor induced ordering of S-loop. A: Surface drawing showing the packing of CpGAPDH subunits A and D in the apoenzyme. A loop comprising of residues 185–197 is disordered in the apoenzyme structure. CpGAPDH holoenzyme structure in which the above mentioned loop is ordered (shown in cyan), is superposed on the apoenzyme structure. B: Surface representation of the interface between subunits A and D of CpGAPDH. A and D subunits of apo-CpGAPDH and Holo-CpGAPDH superposed. The S-loop, which is disordered in the apoenzyme structure but ordered in the holoenzyme, is shown as surface colored by charge (red: negative, blue: positive, green: neutral). Interactions occur between molecules A & D and B & C.

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