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Figure 2.
Figure 2 The internal pseudo-dyad in human EMAPII coincides with
the 2-fold axis in bacterial CsaA. (A) Stereoview of EMAPII (in
violet) superimposed onto itself (in orange), with
superimposable regions shown as thick lines. The pseudo 2-fold
axis is shown by an arrow. (B) The C-terminus domain of EMAPII
(in yellow) is related by 2-fold symmetry to a subset of the OB
fold (in dark violet). (C) Crystal structure of CsaA from
T.thermophilus (Kawaguchi et al., 2001). A subset of the
N-terminus of the symmetrical subunit (in yellow) matches the
C-terminus domain of EMAPII. Orientations in (A), (B) and (C)
are as in Figure 1A. (D) Structure-based sequence alignment of
the C-terminal domain of EMAPII with its N-terminus domain and
with the symmetry-related subunit of CsaA. Helices and strands
are on a coloured background, with helices boxed. The C-domain
of EMAPII is superimposable as a continuous peptide. Dots
indicate residues of EMAPII (N-terminal domain) or CsaA
(symmetry-related subunit) that superimpose with the C-terminus
domain within a 2.5 Å cutoff; numbers indicate the length of
non-superposable intervening sequences.
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