Extended Data Fig. 10: Precursor and nucleotide binding induces conformational change of PsnB. | Nature Chemical Biology

Extended Data Fig. 10: Precursor and nucleotide binding induces conformational change of PsnB.

From: Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB

Extended Data Fig. 10

a, Surface models of the leader-binding domain without (left) or with (right) the bound Phe15 in the LP (magenta sticks). Hydrophobic pocket for Phe15 is shown as magenta dashed lines. b, The nucleotide (cyan sticks) binding shifts the β9β10 loop (from gray to yellow cartoon). Lys172 and Thr180 that interact with a nucleotide are shown as green sticks. c, Two α3α4 pairs of a PsnB dimer show extensive interactions to each other to form a rigid body. Two PsnB subunits are shown as yellow and pale cyan cartoons, and their interacting residues are presented as orange and cyan sticks, respectively. d, Surface model of the ENLC-E complex (yellow and pale cyan for two PsnB subunits). Binding of LP (magenta) and nucleotide (cyan spheres) induces the conformational change of PsnB dimer to generate a compact core (green) binding site. e, Superposition of four LP and CP pairs from PsnB-MP-ADP (7DRM, green and cyan ribbons) and PsnB-MP-AMPPNP (7DRN, magenta and yellow ribbons). All LPs and CPs are well overlapped. PsnB is shown as gray cartoon and half-transparent surface. Nucleotide and Arg213 are shown as gray sticks. Glu37 in CP is shown as sticks.

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