Skip to main content
Fig. 1 | BMC Plant Biology

Fig. 1

From: Florigen and its homologs of FT/CETS/PEBP/RKIP/YbhB family may be the enzymes of small molecule metabolism: review of the evidence

Fig. 1

Spatial organization of the conserved residues forming putative catalytic center in FT protein from Arabidopsis thaliana (PDB ID 1wkp). The three-dimensional structures of proteins were visualized, and their approximate charge-smoothed electrostatic surface representations were generated using the open-source PyMOL environment (Schrödinger LLC; SciCrunch RRID SCR_000305), installed from source using homebrew on the MacOS High Sierra 10.13.6. Top panel: strands are rendered in yellow, helices in light blue, and conserved residues involved in forming the putative enzyme active center are labeled and colored as follows: blue, two conserved aspartates; cyan, two conserved histidines; dark blue, conserved arginine; red, frequently conserved prolines. The loop between strands 3 and 4 is reduced to a short broken wire to improve the visibility of the active center, and the loop that is a major determinant of the differential activity of FT and its paralog TFL1 [4] is rendered as sticks. Bottom panel: The putative enzyme active center rendered as a surface. A rough calculation of the surface electrostatic properties in the vacuum was performed using PyMOL function generate → vacuum electrostatics. The shades of red and blue indicate, respectively, negative and positive charges. The conserved residues involved in forming the putative enzyme active center are labeled, and their colors are the same as in the top panel

Back to article page