 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](gx5204fig3mag.jpg)
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Figure 3
(a) Structure of the 3-MeA–TAG complex (C atoms, yellow; N atoms, blue; O atoms, red) showing the key interactions. The apo structure is shown with C atoms in white. (b) Structure of the 3-MeA–Y16F TAG complex (C atoms shown in pink); the 3-MeA ring adopts a different orientation in the mutant. The 3-MeA in the native protein is also shown. (c) The most common tautomer of 3-MeA could be recognized by a specific hydrogen-bond arrangement of Tyr16 and Glu38. The predominant tautomer of protonated 3-MeA and adenosine would not match this hydrogen-bonding arrangement. (d) DNA damage leads to formation of the positively charged tautomer that is optimal for recognition by TAG; in addition, the highly electron-deficient ring would interact favourably with the TAG active site. |
![[Figure 3]](gx5204fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
