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Figure 4.
Figure 4. (a) A representation of one Fe-protein monomer colored according to rms deviation in C
a
position, follow-
ing superposition of the four AV2 and CP2 subunits. Residues with high rms deviation, such as the C terminus, are
indicated in red; regions of strong structural conservation, such as the b-sheet, are indicated in dark blue. (b) A rep-
resentation of one Fe-protein monomer colored according to amino acid residue conservation, following alignment of
59 Fe-protein sequences. Residues in red, such as the C terminus, indicate the regions of greatest sequence variability;
those in dark blue, such as the 4Fe:4S cluster ligands, P-loop, Switch I and Switch II residues, indicate regions of
strongest sequence conservation. In both (a) and (b), the view is from the dimer interface, and Av2 residue numbers
are included for reference.
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