Fig. 2: Conformation changes on the active site of PLP-bound CrmG and apo CrmG. | Communications Biology

Fig. 2: Conformation changes on the active site of PLP-bound CrmG and apo CrmG.

From: Structural studies reveal flexible roof of active site responsible for ω-transaminase CrmG overcoming by-product inhibition

Fig. 2: Conformation changes on the active site of PLP-bound CrmG and apo CrmG.

a Structure of the active site in PLP-bound CrmG (PDB code 5DDS). The structure is presented as cartoon (upper panel) and surface (lower panel). The active site entrance or opening is labeled with dash circle. Monomer 1 is shown in deep green and monomer 2 is shown in light green. PLP is shown as orange stick. Catalytic base K344 is shown as yellow stick. Residues S206-V212 colored purple blue, residues G213-S232 colored magenta. b One of the four active sites of apo CrmG in C2 space group. Residues S206-H208 colored purple blue, disordered residues G209-P233 in monomer 1 and V369′-H371′ in monomer 2 are shown as red dash line. c The closed form active site of apo CrmG in I222 space group. Coloring scheme same as in a. d Comparison of β10/α10 loop and K344 on apo CrmG (pink) with that on PLP-bound CrmG (deep green). e PLP induces the rearrangement and stabilization of active site in PLP-bound CrmG. Cation–π interaction is indicated with green dash line.

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