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. Author manuscript; available in PMC: 2023 Jul 18.
Published in final edited form as: ACS Synth Biol. 2019 Jun 10;8(6):1314–1324. doi: 10.1021/acssynbio.8b00528

Figure 1. NIRW-ACs design.

Figure 1.

(a) Domain architecture of the first (IlaC), second (IlaD), and third (IlaM) generations of NIRW-ACs. AC (type III AC catalytic domain), GAF, PAS, PHY, GGDEF (diguanylate cyclase catalytic domain), and HK (histidine kinase) are domain designations. The chromophore BV is covalently bound to the Cys residue in the PSM. (b) Chimeric Bph engineering. Shown are X-ray structures of the D. radiodurans BphP PSM (PAS-GAF-PHY) in its dark (left, PDB 4O0P) and light-activated (right, PDB 4O01) forms. Also shown are structures of M. tuberculosis AC RV1264 in the inactive (left, PDB 1Y10) and active (right, PDB 1Y11) conformations. The α-helices extending from the PSM are linked to the output AC modules to generate light-activated enzymes. (c) NIRW-AC protein sequences at the fusion of the PSM and AC modules. The amino acid colors correspond to the colors of protein domains shown above the protein sequences. PSM modules are shown in red (BphP) or grey (BphG1); AC domains are shown in violet (CyaB1) or blue (RV1264); added interdomain linkers are shown in green.