Fig. 2: SAXS and cryo-EM demonstrates that guanine nucleotides bind to human TG2 in the closed state. | Communications Biology

Fig. 2: SAXS and cryo-EM demonstrates that guanine nucleotides bind to human TG2 in the closed state.

From: Distinct conformational states enable transglutaminase 2 to promote cancer cell survival versus cell death

Fig. 2

a, b Titration of 0 to 5 mM GTP into wildtype TG2 (TG2 WT). a The Kratky plot of TG2 for the titration series from 0 mM (dark blue) to 5 mM GTP (dark green). b The Guinier Rg decreases as TG2 adopts a compacted, saturated conformational state. The experimental molecular weight calculated from the Porod Volume is shown on the secondary Y-axis (red). c The scattering profiles of human TG2 expressed in E. coli (dark blue) undergo a similar change when treated with 5 mM GDP (orange) or 5 mM GTP (green). The Guinier Rg and I(0) are shown in the legend. d Nucleotide bound TG2 can be described as a closed state monomer in solution, as demonstrated using CRYSOL to fit to the crystal structure of TG2 bound to GTP (black, PDB ID: 4PYG). The SAXS envelope is shown in light blue. The Guinier Rg and the model Χ2 are shown in the legend. e The 3.2 Å cryo-EM structure of TG2 bound to GDP confirms that GDP bound TG2 is monomeric and adopts the closed state. The cryo-EM map is colored by TG2 domain and map density for the GDP binding site within is shown in the inset.

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