Figure 2.
FIG. 2. Subunit relationships among glycogenin crystal
forms. A, tetrameric association formed by crystallographic
contacts between the dimers that comprise the asymmetric unit in
the 270 crystals. Each
subunit is colored differently, and the position of Tyr-194 in
each subunit is highlighted using purple space-filling atoms,
and the position of the bound UDP molecules is highlighted using
blue space-filling atoms. B, alignment of the dimer formed by
one of the crystallographic axes in the I222 space group (red)
with the dimer of the 270 enzyme that
comprises the asymmetric unit of the P6[4] space group (yellow).
For this figure only the respective "A" subunits were aligned.
The red arrow indicates the amount of additional rotation
required to align the "B" subunits using the molecules oriented
in this manner. Figure was prepared using the programs MOLSCRIPT
(38) and Raster3D (39, 40).
The above figure is reprinted
from an Open Access publication published by the ASBMB:
J Biol Chem
(2005,
280,
23892-23899)
copyright 2005.
270 crystals. Each
subunit is colored differently, and the position of Tyr-194 in
each subunit is highlighted using purple space-filling atoms,
and the position of the bound UDP molecules is highlighted using
blue space-filling atoms. B, alignment of the dimer formed by
one of the crystallographic axes in the I222 space group (red)
with the dimer of the