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Figure 2.
Figure 2: Structure of BluB. a, Ribbon diagram of BluB
with FMN in the binding pocket (stick representation). The
two-fold axis is perpendicular to the plane of the figure. b, E.
coli nitroreductase NfsB (Protein Data Bank 1ICR)^21 with FMN
and nicotinic acid (stick representation) in the binding pocket.
c, Cross-section of BluB's molecular surface. The two-fold axis
lies along the y axis such that the si-face of FMN is viewed on
the left and re-face on the right. The surface is coloured
according to electrostatic potential, where blue is
electropositive, red is electronegative and k[B] is Boltzmann's
constant. The back and front of the surface are cut away to
reveal the FMN binding pocket buried in the dimer interface. The
pocket wraps snugly around FMN, preventing interaction with
other substrates. d, The BluB ribbon diagram has been coloured
according to B-factor. Red represents flexible regions that may
control or gate access to the active site.
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