Figure 5.
Figure 5. Structural differences between ZmHP2 molecules in
the asymmetric unit around the loop connecting the four-helix
bundle with the N-terminal helices. Compared to Figure 1 Go-, this
figure is rotated by 90 degrees around the horizontal axis.
Since the structures of the monomers of each pair of ZmHP2
molecules in the asymmetric unit are essentially the same, only
molecules A1 (green) and B1 (purple) are shown. Oxygen, nitrogen
and sulfur atoms are shown in red, blue and green, respectively.
Hydrogen bonds and salt bridges are indicated by dots. In
molecule A1, residues 35-38 are indicated in yellow. Gly41 in
molecule A1 and three glycine residues (37, 38, and 41) in
molecule B1 are colored pink. The residues of molecule A1
involved in packing interactions with molecule B1 in the crystal
are shown in cyan.
The above figure is reprinted
by permission from the Protein Society:
Protein Sci
(2005,
14,
202-208)
copyright 2005.
, this
figure is rotated by 90 degrees around the horizontal axis.
Since the structures of the monomers of each pair of ZmHP2
molecules in the asymmetric unit are essentially the same, only
molecules A1 (green) and B1 (purple) are shown. Oxygen, nitrogen
and sulfur atoms are shown in red, blue and green, respectively.
Hydrogen bonds and salt bridges are indicated by dots. In
molecule A1, residues 35-38 are indicated in yellow. Gly41 in
molecule A1 and three glycine residues (37, 38, and 41) in
molecule B1 are colored pink. The residues of molecule A1
involved in packing interactions with molecule B1 in the crystal
are shown in cyan.