Fig. 5 | Nature Communications

Fig. 5

From: The structural basis of N-acyl-α-amino-β-lactone formation catalyzed by a nonribosomal peptide synthetase

Fig. 5

Structure of ObiF1 TE domain. a The ObiF1 TE domain (red) is adjacent to the C domain (blue); active site residues that were targeted for mutation are highlighted. b Catalytic triad residues Cys1146, His1284, and Asp1254. In ObiF1, Gly1173 occurs at the β-strand 5 position where the aspartic acid residue is typically found in the His-Asp dyad of EntF-like TE domains. c The ObiF1 TE domain (red) contains a three-helix lid-loop region (cyan). d ObiF1 TE domain (red) is superimposed with the RifR type II TE domain (3FLB; gray) using PyMol

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