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Figure 3.
Overall crystal structure of mFMO. (A) Ribbon diagram of the
monomer. FAD-binding domain (residues 8–169 and 281–450) is
orange and NADP-binding domain (residues 170–280) is green.
FAD is shown as yellow sticks and NADP^+ as blue sticks. The
positions of the long interdomain loop (residues 44–80), the
hinge connecting the two domains, and the polypeptide stretch
corresponding to residues 407–415 are outlined. mFMO residues
corresponding to TMAU-causing mutations (17) and polymorphisms
in hFMO3 (in parentheses) are in red and blue sticks,
respectively. The position of a long insert in hFMO3 (residues
238–299; Fig. 1B) is also indicated. It is expected to occupy
a surface-exposed position away from the active site. (B) Ribbon
representation of the mFMO dimer. One monomer is shown in the
same orientation and color as Fig. 3A; the other one is colored
gray, with the NADP-binding domain in darker gray.
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