Fig. 3: Structure and mechanism of CalA3 KS ___domain. | Nature Communications

Fig. 3: Structure and mechanism of CalA3 KS ___domain.

From: C–N bond formation by a polyketide synthase

Fig. 3

a Structure of KS dimer, shown in ribbon representation. b Close-up view of the disconnected, double open-ended substrate tunnels. The atomic model of KS ___domain is shown here in mesh representation. Selected residues in (c-d) are shown as sticks. c Left, tunnel-intercepting aromatic residue pair. Right, superposition of CalA3 KS with DEBS module 5 and mFAS KS domains reveals a loop that shifts relatively 15.3 and 14.1 Å distance, respectively. d Superposition of the conserved Cys-His-His active site residues reveals a 143° side-chain rotation of C197 in CalA3 KS ___domain. The potential hydrogen bonds between C197-H372 and C197-C436 are indicated with yellow dashed lines and the distances are labeled (Å). e HPLC traces at λ = 290 nm showing the products of the in vitro reactions catalyzed by CalA3 WT or mutants.

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