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Figure 1.
Figure 1. Overall structure of mouse AIF. a, Structural
comparison of AIF, GR and BphA4. FAD and NADH are shown in black
and cyan sticks, respectively. b, Crystallographic contacts in
AIF crystals. Monomers 2 and 3 form a crystallographic dimer
related by a two-fold axis. The Pro-rich C-terminal insertion is
stabilized by crystal contacts, as seen between monomers 1 and
2. c, Distribution of invariant residues (green) among mammalian
and D. discoideum AIFs in both faces of the monomer. The FAD
molecular surface is shown in magenta. The dimerization area is
marked and the two-fold axis is depicted by an arrow.
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