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Fig. 3 | Microbial Cell Factories

Fig. 3

From: Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Fig. 3

Crystal structure of SfSFGH. a The overall structure of SfSFGH is shown as a ribbon diagram with α-helices (aquamarine color) and β-strands (salmon color). The catalytic triad residues (Ser148, Asp24, and His257) are shown as stick models. b Multiple sequence alignments of SfSFGH (NCBI reference sequence number WP_011638859.1) with homologous models. The sequences of esterases from the oil-degrading bacterium Oleispira antarctica (PDB code 3i6y; UniProtKB code D0VWZ4), S-formylglutathione hydrolase from Pseudoalteromonas haloplanktis (PDB code 3ls2; UniProtKB code Q3IL66), S-formylglutathione hydrolase from Agrobacterium tumefaciens (PDB code 3e4d; UniProtKB code A9CJ11), esterase D from humans (PDB code 3fcx; UniProtKB code P10768), esterase D from Neisseria meningitides (PDB code 4b6g; UniProtKB code Q9JZ43), and S-formylglutathione hydrolase from Saccharomyces cerevisiae (PDB code 1pv1; UniProtKB code P40363) were used for alignment. The conserved motif found in SFGHs is boxed in red. The catalytic triad residues indicated with a black triangle are conserved in all models. The gatekeeper residue of tryptophan is indicated with a black circle. An alignment was prepared using the program ClustalX and edited with GeneDoc. Corresponding secondary structures are shown above the sequences

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