|
Figure 4.
Figure 4. Surface representation of the TET complex, colour
coded according to its electrostatic potential contoured from
-15 kT/e (intense red) to 15 kT/e (intense blue). (a) Stereo
representation of the oligomeric TET complex. The molecule is
oriented along its 3-fold symmetry axis with the central opening
facing the reader. (b) Two halves of the complex in cut-open
surface representation, viewed along the 3-fold axis. The
central pore, indicated by the grey surfaces, measures about 60
Å in diameter. Inhibitor molecules (green) are bound to
the active centres, Zn2+ atoms are coloured in magenta. Left:
The three openings for exit of the produced amino acids (9
Å in diameter) are clearly seen in proximity to the
central opening (18 Å in diameter). Right: the cluster of
positively charged arginine residues (blue, in the centre)
facilitates redirection of the substrate peptides' amino termini
to the adjacent positively charged specificity pockets (red,
with bound inhibitor).
|
