Skip to main content


Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Fig. 1 | BMC Research Notes

Fig. 1

From: Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation

Fig. 1

The structure of dUTPase. a The structure of Arabidopsis dUTPase with an inhibitor bound at the active site. The cylinders in each subunit represent only one helix, which contains Ser89 and Trp93. b Each subunit shows five conserved motifs. The five conserved motifs (M1–M5) are highlighted in gray in the holo Arabidopsis dUTPase chain B. c Sequence alignment of dUTPase. The five conserved motifs are indicated by gray shading. Ser89 and Trp93 are boxed. The secondary structure of chain B in the holo Arabidopsis dUTPase, which was identified using DSSP [27], is indicated by the lowercase letters in the top line; ‘e’, β-strand; ‘t’, hydrogen bonded turns; ‘s’, bend; and ‘h’, α-helix. The coordinates of the underlined amino acid residues were not modeled (Table 1). d Estimation of kinetic parameters. Five independent data sets were plotted with different symbols. The inset graph shows the integrated Michaelis–Menten equation fit to the absorbance data shown. The solid line in the figure shows the best-fit line used to estimate the K m value

Back to article page