Extended Data Figure 5: Structure of OxyBtei and multiple sequence alignment of the Oxy enzymes. | Nature

Extended Data Figure 5: Structure of OxyBtei and multiple sequence alignment of the Oxy enzymes.

From: X-domain of peptide synthetases recruits oxygenases crucial for glycopeptide biosynthesis

Extended Data Figure 5

a, Structure of OxyBtei determined in complex with the X-domain. Secondary structure elements are labelled and coloured grey with the following exceptions: B-helix and loop region (magenta), D-helix (cherry red), E-helix (blue), F-helix (orange), G-helix (yellow), I-helix (cyan), β1-sheet (green), β2-sheet (purple), β3-sheet (orange), β4-sheet (yellow), haem shown as sticks (C atoms, red; N atoms, blue; O atoms, orange) with the haem iron shown as a red sphere. b, Sequence alignment of Oxy proteins from Actinoplanes teichomyceticus teicoplanin gene cluster23,24. Secondary structure and colour scheme same as a; catalytic residues are shown in orange; residues important for X-domain interaction are indicated in the three boxed regions, are in bold and highlighted in yellow for OxyBtei. Colours used for the corresponding residues from OxyAtei, OxyCtei and OxyEtei indicate agreement with the consensus sequence (green, match; blue, comparable interaction; red, potential mismatch).

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