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Table 1 Comparison of secondary structures and interactions at the ligand-binding site

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

  A. thaliana S. cerevisiae H. sapiens E. coli M. tuberculosis
Sequence similaritya Self 56.2 % 63.9 % 35.5 % 39.2 %
K m 0.4 ± 0.1 μM 13.2 ± 0.6 μM 3.6 ± 1.9 μM 0.5 μM
(SE 17 %)
0.46 ± 0.2 μM
α helix 1st res S89 S69 S86 S72 S65
α helix 5th res W93 V73 A90 H76 T69
α1st–WAT–α5th Present Absent Absent Absent Absent
References This study Tchigvintsev et al. [19] Toth et al. [15] Barabas et al. [11] Pecsi et al. [17]
  1. α1st–WAT–α5th refers to the presence of an interaction among the first residue of the α helix, a water molecule, and the fifth residue of the α helix
  2. aSequence similarities between Arabidopsis and each species were calculated by using SIM [28] on the ExPASy server (