Fig. 2: EPR spectroscopic characterization and AlphaFold2 predicted structure model of Gms. | Nature Communications

Fig. 2: EPR spectroscopic characterization and AlphaFold2 predicted structure model of Gms.

From: Biosynthesis of GMGT lipids by a radical SAM enzyme associated with anaerobic archaea and oxygen-deficient environments

Fig. 2

a, b Domain organization (a) and the overall architecture of Gms (b) showing an N-terminal domain comprised of six helices, a conserved RS domain, a bridging region with two helices, a β-harpin motif, and a C-terminal SPASM domain. c The interaction between the β-hairpin and the pocket involves two hydrogen bonds between F326 and N351, as well as between S334 and E346. d Cavity map for the active site of Gms reveals the hydrophobic pocket. e Representations of the three [4Fe–4S] clusters in the structure model of Gms. Protein is shown as a cartoon, SAM, and [4Fe–4S] clusters are shown in ball-and-stick models. f X-band CW EPR spectra of various Gms samples (i) the wild-type (WT) Gms reduced by DTH; (ii) subsequently adding SAM to DTH-reduced Gms; (iii) the mutant sample of Gms (C438AC370AC372A) containing only radical SAM (RS) cluster reduced by DTH, and incubated with SAM; (iv) the mutant sample of Gms (C438AC123AC127A) containing only AuxI cluster reduced by DTH; (v) the mutant sample of Gms (C123AC127A C370AC372A) containing only AuxII cluster reduced by DTH. Black, blue and green traces are experimental spectra, and the red traces are simulated spectra.

Back to article page