Biology Reference
In-Depth Information
Figure 3.1 The MaPgb
*
fold. (A) Tertiary structure of MaPgb
*
. Secondary structure ele-
ments conforming to the classical 3/3 globin fold are shown in white (labels A through
H). Structural elements specific of MaPgb
*
are displayed in grey (Z-helix) and in black
(N-terminal, CE and FG loops). (B) The N-terminal region, the CE and FG loops bury the
haem (black) and prevent access of small ligands to the haem distal cavity, which is con-
nected to the solvent region by tunnel 1 and tunnel 2 (grey mesh). (C) Quaternary struc-
ture of MaPgb
*
. The two MaPgb
*
subunits within the dimer, interacting mainly through
the G- and H-helices (helical bundle), are shown in white and grey (haem in black).
