Comparison of Cg-OxyR active-site pocket with previously published structures. Comparison of Cg-OxyR active-site pocket with previously published structures.

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Comparison of Cg-OxyR active-site pocket with previously published structures. Comparison of Cg-OxyR active-site pocket with previously published structures. (A) OxyR structures show conservation of the active-site region. The active-site architecture from the OxyR crystal structures of C. glutamicum C206S (present study), V. vulnificus E204G OxyR2 [PDB ID code 5B7D (25)], N. meningitidis [PDB ID code 3JV9 (24)]*, P. gingivalis C199S [PDB ID code 3T22 (26)], and P. aeruginosa [PDB ID code 4Y0M (23)] are shown. (B) Comparison of the different H2O2 binding modes of the H2O2-soaked crystal structures of C. glutamicum OxyRC206S (present study) and P. aeruginosa C199D [PDB ID code 4X6G (23)]. Polar interactions between the residue side-chains and ligands (SO42−, H2O2) or water molecules (red spheres) are presented as dashed black lines. *The crystal structure of N. meningitidis OxyR contains two protein chains; in the active-site pocket of the alternate protein chain (not shown), the conserved water molecule which hydrogen bonds R270 is present but the conserved water molecule hydrogen bonding T129 is absent. Brandán Pedre et al. PNAS doi:10.1073/pnas.1807954115 ©2018 by National Academy of Sciences