Figure 5.
Figure 5. Differences in K4 conformation in the different
methylation states. (a–d) The crystal-packing interface
relevant to K4 conformation is depicted for the H3K4me3 complex
(C2 space group, a), H3K4me2 complex I (C2, b), H3K4me1 complex
(C2, c) and unmodified H3 complex (P2[1], d). Peptides are
colored as in Figure 2b; the principal WDR5 protomer is red; and
the symmetry-related protomer at the peptide interface is gray.
Note the rotation about 3
moving from the tri- and dimethylated species to the
monomethylated and unmodified species. In H3K4me2 complex I, the
distances between the -methyl
carbons and the Glu322 carboxylate O 1
are 3.27 Å and 3.37 Å for the closest methyl group
in each of the two complexes per asymmetric unit, whereas these
distances are 3.83 Å and 3.87 Å for the more distant
methyl group. For comparison, the previously reported shorter
distances for these measurements were 3.15 Å and 3.42
Å^22.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2006,
13,
704-712)
copyright 2006.
3
moving from the tri- and dimethylated species to the
monomethylated and unmodified species. In H3K4me2 complex I, the
distances between the 
-methyl
carbons and the Glu322 carboxylate O 
1
are 3.27 Å and 3.37 Å for the closest methyl group
in each of the two complexes per asymmetric unit, whereas these
distances are 3.83 Å and 3.87 Å for the more distant
methyl group. For comparison, the previously reported shorter
distances for these measurements were 3.15 Å and 3.42
Å^22.