Extended Data Fig. 7: DRT1 RT active site and comparison of the DRT1 nitrilase domain.
From: Semirandom DNA adducts regulate a filamentous defense-associated reverse transcriptase
a) DRT1 with dATP substrate in the RT active site. Electron density for the dATP substrate shown as mesh contoured at threshold: 0.169. b) Electrostatic surface representation of the DRT1 RT active site pocket. c) Superposition of the DRT1 α′ protomer nitrilase domain (residues 934-1229) (pink) with protomer 1 of yeast Nit2 (PDB: 4HG5) (teal) ‘closed lid’ conformation. Oxaloacetate substrate of Nit2 protomer 1 is shown in magenta, and nitrilase catalytic triad residues of both proteins are shown as sticks. d) Superposition of the DRT1 α′ protomer nitrilase domain (residues 934-1229) (pink) with protomer 1 of Syechocystis sp. nitrilase (PDB: 3WUY) (yellow) ‘open lid’ conformation. Nitrilase catalytic triad residues of both proteins are shown as sticks. e) Surface representation of the DRT1 nitrilase active site pocket formed between protomers α′ and α. There is approximately 12 Å between the catalytic C1116 of α′ and T1220 on the α lid.
