|
Figure 1.
Fig. 1. Structure of the CMG2 VWA domain. A ribbon diagram
of the S38 structure indicates secondary structure elements.
Highlighted amino acid residues include the N- and C-terminal
cysteines (C39 and C218, respectively) that form a disulfide
bond (the sulfur atoms are depicted in yellow) and the conserved
amino acids of the MIDAS motif. The Mg2+ ion is shown as a large
blue sphere with two bound water molecules depicted as beige
spheres. The small red spheres correspond to oxygen atoms within
the MIDAS amino acids. The E194 residue from a neighboring CMG2
molecule (only E194 is shown in pink) contributes the sixth
coordinating residue at the MIDAS metal. The structures of S38
and R40 superimpose with an rms deviation of 0.7 Å2. They
differ primarily in the orientation of the  6 C-terminal helix.
This helix and its preceding loop in the R40 structure are
depicted in blue. This image and Fig. 3 were generated by the
program MOLSCRIPT (47) and rendered in RASTER3D (48).
|
