Figure 1.
Fig. 1. Cdc4p is composed of two structurally distinct
domains connected by a flexible linker. Shown is the ensemble of
26 structures calculated for the wild-type protein, superimposed
using the backbone atoms in the -helices of
the N-terminal domain (A, all residues; B, residues 2-66 only),
and the C-terminal domain (C, residue 77-141 only). Due to the
flexible linker, the N- and C-terminal domains do not have a
fixed orientation with respect to one another. A MOLSCRIPT
ribbon diagram of one representative structure of Cdc4p is shown
in D, with -helices
colored as in A-C and -strands
indicated as white arrows. Helix boundaries are as follows: A
(8-14), red, B (26-35), orange, C (41-49), yellow, D (58-64),
green, E (79-86), green, F (96-105), blue, G (113-119), purple,
and H (133-137), magenta. The short anti-parallel -sheets
encompass residues 22-24 and 54-56 in the N-terminal domain and
93-95 and 127-129 in the C-terminal domain. Also indicated in D
are the positions of point mutations in the N- (F12L, G19E, and
R33K) and C-terminal domains (F79S, G82D, and G107S) causing
temperature-dependent cell growth arrest at cytokinesis. Serines
2 and 6, which are sites of phosphorylation in vivo (40), lie at
the exposed N terminus of the protein.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
5943-5951)
copyright 2001.
-helices of
the N-terminal domain (A, all residues; B, residues 2-66 only),
and the C-terminal domain (C, residue 77-141 only). Due to the
flexible linker, the N- and C-terminal domains do not have a
fixed orientation with respect to one another. A MOLSCRIPT
ribbon diagram of one representative structure of Cdc4p is shown
in D, with 
-strands
indicated as white arrows. Helix boundaries are as follows: A
(8-14), red, B (26-35), orange, C (41-49), yellow, D (58-64),
green, E (79-86), green, F (96-105), blue, G (113-119), purple,
and H (133-137), magenta. The short anti-parallel