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Figure 2.
Figure 2. Structure of Sulfite Oxidase(A) The monomer with
the N-terminal domain drawn in red, the Mo-co domain in yellow,
and the C-terminal domain in green. The N and the C termini are
labeled with N and C, respectively. The dotted line between
domains I and II indicates the loop region, which is only weakly
defined in the electron density. The Mo-co and the heme are
shown in ball-and-stick representation with the Fe atom in
purple and the Mo atom in green. Figure 2 and Figure 3B have
been generated with the programs MOLSCRIPT ( [30]) and RASTER3D
( [1 and 34]).(B) Cα trace of the sulfite oxidase dimer. The
gray dotted lines connect the metal centers of the cofactors and
indicate the distances between the Mo and Fe within the monomer
and the Mo-Mo distance between the two monomers.(C) Interface
between the N-terminal and the Mo-co domain. Aliphatic residues
are shown in all-bonds representation whereas the heme and
residues involved in hydrogen bonding are shown in
ball-and-stick representation. Dotted lines indicate hydrogen
bonds.
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