Figure 4
PMP-incorporated active site of Tr-ωTA. (a) Active site cavity of Tr-ωTA. The PMP cofactor is positioned in the vicinity of the interface of the two subunits. Some residues from subunit A are involved in the formation of the active site of subunit B. The apo enzyme and PMP are represented as surface and stick (green) modes, respectively. Subunit A and B are colored orange and cyan, respectively. (b) A cross section representing a funnel to the active site. The PMP cofactor is located in the bottom of the long funnel. Tr-ωTA is depicted as a surface (white) mode. (c) Omit map of PMP and Lys289. The omit map (FO–FC) is colored magenta and contoured at the 2.0 sigma level. (d) UV-Visible spectrum of Tr-ωTA. The red arrow indicates the peak position at approximately 330 nm. (e) The P- and O-pockets in the active site. The apo enzyme except for the active site (yellow surface and sticks) is represented in ribbon. Subunits A and B are colored orange and cyan, respectively. The asterisk of the F89 residue denotes a residue from the other subunit.
