Fig. 2: Protein structure and engineering of SgvM toward a general enantioselective methylation biocatalyst. | Nature Communications

Fig. 2: Protein structure and engineering of SgvM toward a general enantioselective methylation biocatalyst.

From: A biocatalytic platform for asymmetric alkylation of α-keto acids by mining and engineering of methyltransferases

Fig. 2

a Phylogenetic analysis and evaluation of wt CMTs. Original organism: MarI: Streptomyces sp. B9173, MppJ: S. hygroscopicus, SgvM: S. griseoviridis, CdpJ: Chondromyces crocatus. b Overview of the structure of wt SgvM. c SgvM in complex with α-ketoleucine and methylthioadenosine (MTA). A simulated annealing omit map with ligand coordinates omitted is superimposed at 3σ above background in blue wire-mesh. d SgvM in complex with α-ketoleucine and S-adenosylhomocysteine (SAH). A simulated annealing omit map with ligand coordinates omitted is superimposed at 3σ above background in blue wire-mesh. e Superposition of the SAH- and MTA-bound structures of SgvM. f Structure-guided engineering of SgvM: development of the triple mutant SgvM F329V T331A M144V (SgvMVAV). Reactions were performed in triplicates and data are shown as mean ± SD (n = 3).

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