Figure 4.
Figure 4: Active site and mechanism of JMJD2A. a, Stereoview
omit 2F[o]-F[c] electron density maps contoured at 1 for
H3K9me3 (blue) and H3K9me1 (red). The positions (a, b, c) for
the three methyl groups of the H3K9me3 substrate are indicated
with b projecting towards the metal-bound water. In the H3K9me1
structure the methyl group occupies position a with two water
molecules (W1 and W2) close to the b and c positions. b, Outline
of the catalytic cycle for JMJD2A showing the proposed ferryl
and hemiaminal intermediates. Oxygen may bind at the position
trans to His 276 or His 188.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2007,
448,
87-91)
copyright 2007.
for
H3K9me3 (blue) and H3K9me1 (red). The positions (a, b, c) for
the three methyl groups of the H3K9me3 substrate are indicated
with b projecting towards the metal-bound water. In the H3K9me1
structure the methyl group occupies position a with two water
molecules (W1 and W2) close to the b and c positions. b, Outline
of the catalytic cycle for JMJD2A showing the proposed ferryl
and hemiaminal intermediates. Oxygen may bind at the position
trans to His 276 or His 188.