Figure 2.
Figure 2. Stereo picture of the biosynthetic thiolase
tetramer with its "tetrahedral cage" tetramerization motif. The
tetramer is colored according to the B-factor of the C^a atom of
each residue. Dark blue corresponds to a B-factor of vert,
similar 5 Å2; red corresponds to 100 Å2. The A-B
dimer (upper half of the Figure) has significantly lower
B-factors than the C-D dimer (lower half). This is a result of
the layered packing in the crystal lattice [Modis and Wierenga
1999]. Four molecules of acetyl-CoA are shown in ball-and-stick
representation, bound to each of the four subunits near the
interface between the A-B and C-D dimers. The side-chains of
residues located in high B-factor loops and pointing towards the
CoA moiety are also shown. These include residues Lys133,
Arg172, Lys208 and Arg232-Pro233-Ala234-Phe235-Asp236-Lys237,
which are all located in the loop domain. Figure 2, Figure 5 and
Figure 6 were prepared with MOLSCRIPT [Kraulis 1991] and
Raster3D [Merritt and Bacon 1997].
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2000,
297,
1171-1182)
copyright 2000.
vert,
similar 5 Å2; red corresponds to 100 Å2. The A-B
dimer (upper half of the Figure) has significantly lower
B-factors than the C-D dimer (lower half). This is a result of
the layered packing in the crystal lattice [Modis and Wierenga
1999]. Four molecules of acetyl-CoA are shown in ball-and-stick
representation, bound to each of the four subunits near the
interface between the A-B and C-D dimers. The side-chains of
residues located in high B-factor loops and pointing towards the
CoA moiety are also shown. These include residues Lys133,
Arg172, Lys208 and Arg232-Pro233-Ala234-Phe235-Asp236-Lys237,
which are all located in the loop domain. Figure 2, Figure 5 and
Figure 6 were prepared with MOLSCRIPT [Kraulis 1991] and
Raster3D [Merritt and Bacon 1997].