Fig. 2: BRD1389 binds at the active site of Plasmodium cFRS. | Nature Communications

Fig. 2: BRD1389 binds at the active site of Plasmodium cFRS.

From: Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines

Fig. 2: BRD1389 binds at the active site of Plasmodium cFRS.The alternative text for this image may have been generated using AI.

a Structural organization of PvcFRS α- and β-subunits. b Overall structure of PvcFRS showing functional biological heterotetrametric assembly (αβ)2 with two crystallographic heterodimers (αβ). The domain boundaries are labelled according to TtFRS (PDB “2IY5 [https://www.rcsb.org/structure/2IY5]”). The α-subunit consists of two domains: PA1 (catalytic domain, CAT) and PA2 domain. The β-subunit consists of PB1, PB3 (editing domain), PB4, PB5 and PB6-B7 (catalytic-like, CAM). c Surface view of PvcFRS:BRD1389 complex depicting α-subunit (grey), β-subunit (pink) and bound BRD1389 (green) in the α-subunit. d The composite simulated annealed omit (SA-omit) (orange) and the final 2Fo-Fc (blue) maps are contoured at 1 σ levels for the bound BRD1389. The final 2Fo-Fc (blue) map clearly shows the continuous electron density for the bound BRD1389.

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