Figure 1.
Figure 1 Structure of EMAPII. (A) Overall view of human
EMAPII/p43. The five -strands
of the OB fold are in violet, the linker region in orange and
the C-terminal domain in yellow. The His-tag in the C-terminus
is shown as a dotted line. (B) Alignment of sequences of
selected p43 (Hs, Homo sapiens; Dm, Drosophila melanogaster; Eo,
Euplotes octocarinatus; At, Arabidopsis thaliana) and
p43-related proteins (Sc, Saccharomyces cerevisiae; Os, Oriza
sativa; Tp, Treponema pallidum; Ec, E.coli; Aa, A.aeolicus; Tt,
T.thermophilus). Helices (rectangles) and strands (arrows) are
coloured as in (A). Amino acids conserved in >50% of sequences
are boxed in black. Hydrophobic residues at the domain interface
are on a yellow background. The conserved motif in the
C-terminal domain is highlighted in red.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
570-578)
copyright 2001.
-strands
of the OB fold are in violet, the linker region in orange and
the C-terminal domain in yellow. The His-tag in the C-terminus
is shown as a dotted line. (B) Alignment of sequences of
selected p43 (Hs, Homo sapiens; Dm, Drosophila melanogaster; Eo,
Euplotes octocarinatus; At, Arabidopsis thaliana) and
p43-related proteins (Sc, Saccharomyces cerevisiae; Os, Oriza
sativa; Tp, Treponema pallidum; Ec, E.coli; Aa, A.aeolicus; Tt,
T.thermophilus). Helices (rectangles) and strands (arrows) are
coloured as in (A). Amino acids conserved in >50% of sequences
are boxed in black. Hydrophobic residues at the domain interface
are on a yellow background. The conserved motif in the
C-terminal domain is highlighted in red.