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. Author manuscript; available in PMC: 2020 Jun 23.
Published in final edited form as: Nat Struct Mol Biol. 2019 Dec 23;27(1):42–48. doi: 10.1038/s41594-019-0352-5

Fig. 2: Product binding and changes in the tetramer interface in CTPS2 structures.

Fig. 2:

(a) CTPS2 P-state tetramer, colored by monomer. (b) Zoomed-in view of the yellow box in (a), showing ADP (orange) bound in a novel conformation. Cryo-EM density is shown in transparent grey. (c) Comparison of ADP conformations in the CTPS2 P-state filament (color) with existing ADP-bound CTPS structures (grey). ADP in the P-state filament is packed between residues F77 and N73. In other CTPS structures, ADP is bound to a pocket formed by R217 and lid residues 244–250 (dashed blue box). (d) Zoomed-in view of the black box in (a), showing the CTP binding site. (e) Comparison of the tetramer interface around the CTP binding site in the P-state (blue and green) and S-state (grey) structures.