Figure 1.
Figure 1 Overview of the SelB:GDP structure from M. maripaludis.
(A) Structure of SelB molecule C in the GDP conformation. The C
trace
is rainbow coloured from the N- (blue) to the C-terminus
(orange). SelB consists of four individual domains, denoted I,
II, III and IV, which are arranged to form a 'molecular
chalice'. The first three domains form the cup and the fourth
the base of the chalice. The GDP nucleotide (red) is bound to
domain I (blue), which carries the GTPase activity. (B)
Flexibility of domain IV demonstrated by superposition of two
different SelB:GDP molecules (chains A and C) in the asymmetric
unit. The superposition of the first three domains shows that
domain IV is flexibly linked to domain III. Its orientation in
these two snapshots varies by an approximately 20° rotation.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2005,
24,
11-22)
copyright 2005.
trace
is rainbow coloured from the N- (blue) to the C-terminus
(orange). SelB consists of four individual domains, denoted I,
II, III and IV, which are arranged to form a 'molecular
chalice'. The first three domains form the cup and the fourth
the base of the chalice. The GDP nucleotide (red) is bound to
domain I (blue), which carries the GTPase activity. (B)
Flexibility of domain IV demonstrated by superposition of two
different SelB:GDP molecules (chains A and C) in the asymmetric
unit. The superposition of the first three domains shows that
domain IV is flexibly linked to domain III. Its orientation in
these two snapshots varies by an approximately 20° rotation.