journal menu
![[Figure 4]](jv5010fig4mag.jpg)
|
|
Figure 4
Structural changes in mutants from the RDM1 series: RDM1-3 (yellow), RDM1-12 (blue), RDM1-37 (violet), RDM1-8 (magenta), RDM1-24 (salmon), RDM1-29 (light green) and RDM1-38 (dark green). The WT protein, shown for reference, is colored light gray. The mutation sites are marked in frames. Hydrogen bonds are shown as dashed lines and water molecules as spheres. For clarity of viewing, some side chains were omitted in the figures. (a) RDM1-3; Thr207 is hydrogen-bonded to Leu204, while His206 occupies the free space between Glu125 and Glu81. (b) RDM1-3; Gln211 is involved in an extended network of hydrogen bonds, while Pro210 is neutral for the conformation of the neighboring residues. (c) RDM1-12; two nonpolar substitutions at positions 210 (D/A) and 211 (S/A) do not affect the conformation of the adjacent side chains. (d) RDM1-37; a shift of His119 induces a swing of the Glu234 side chain, forcing it form a hydrogen bond to Arg238; in the WT protein Glu234 is hydrogen-bonded to Arg207 and His119. (e) RDM1-8 (chain B); Gln207 forms several water-mediated hydrogen bonds to protein main-chain atoms. (f) RDM1-8 (chain D); Gln207 is hydrogen-bonded to Glu234, which has a different orientation than in chain B. (g) RDM1-24; the substitution R207A is neutral for the conformation of the neighboring side chains. (h) RDM1-24; substitutions D210S and S211T do not affect the position of the catalytic Thr179. (I) RDM1-29; Cys206 is directed away from the active site. (j) RDM1-29; two nonpolar substitutions, S211V and D210L, in the close neighborhood of Thr179. (k) RDM1-38; position and orientation of Cys207 in chain B. (l) RDM1-38; nonpolar substitution of S211V in the close vicinity of the catalytic Thr179. |
![[Figure 4]](jv5010fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
