Fig. 1: Characterisation of the P. stuartii Adc decamer. | Communications Biology

Fig. 1: Characterisation of the P. stuartii Adc decamer.

From: Structural and biochemical characterisation of the Providencia stuartii arginine decarboxylase shows distinct polymerisation and regulation

Fig. 1

a Cryo-EM map of the P. stuartii Adc decamer. Top and clipped side views of the 2.4 Å resolution cryo-EM map are shown, with the clipping plane indicated by dotted lines on the top view. Domains are coloured by domain as shown in the schematic, with amino acid numbers at domain boundaries corresponding to the first residue of each domain. b Crop of a representative micrograph of Providencia stuartii Adc, scale bar = 50 nm. c Cartoon representation of a P. stuartii Adc dimer extracted from the decamer structure. One monomer in the dimer is coloured by domain as per a, the other is coloured light grey. The inset shows a close up of the active site, with active site residues shown as sticks and labelled. The PLP cofactor covalently bound to K386 is shown in yellow. The cryo-EM density for active site residues is overlaid. d Mass photometry characterisation of P. stuartii Adc oligomerisation showing the distribution of species of different molecular weights at pH 4.0, 5.0, 6.5 and 8.0.

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