Figure 1.
Figure 1 Structure of the HMG-box of HMG-D bound to DNA. (A)
Sequence comparison of sequence-specific and
non-sequence-specific HMG domains. The sequences are aligned and
numbered according to the HMG-D structure, with helices, I, II
and II depicted by black boxes (Jones et al., 1994; Baxevanis
and Landsman, 1995). Residues shown from structural and modeling
studies to intercalate the DNA are outlined in black (Love et
al., 1995; Werner et al., 1995a,b; Balaeff et al., 1998; Allain
et al., 1999; Ohndorf et al., 1999). Residues that are conserved
between the two HMG-box families are shaded in gray, whereas
those residues that consistently differ between the two families
of HMG domains are highlighted in cyan and brown (Balaeff et
al., 1998; Churchill et al., 1999). (B) Stereo view of the
refined (2|F[o]| - |F[c]|) electron density map contoured at a
level of 1.9 .
The protein and DNA are colored using standard CPK coloring,
with water molecules and a sodium ion represented by red and
blue spheres, respectively. (C) Ribbon diagram in stereo view of
the complex. HMG-D is depicted in cyan, the DNA in gray, and
structural water molecules found in the protein and at the DNA
interface in red. Several side chains that interact with the
DNA, Ser10, Tyr12, Met13, Asn17, Arg20, Val32, Thr33 and Ala36,
are shown in green. The protein is well ordered from residue 4
to 72, and the DNA is well ordered throughout except for base
cytosine 10, which adopts two conformations in the crystal (only
one conformation is shown).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
6610-6618)
copyright 1999.
.
The protein and DNA are colored using standard CPK coloring,
with water molecules and a sodium ion represented by red and
blue spheres, respectively. (C) Ribbon diagram in stereo view of
the complex. HMG-D is depicted in cyan, the DNA in gray, and
structural water molecules found in the protein and at the DNA
interface in red. Several side chains that interact with the
DNA, Ser10, Tyr12, Met13, Asn17, Arg20, Val32, Thr33 and Ala36,
are shown in green. The protein is well ordered from residue 4
to 72, and the DNA is well ordered throughout except for base
cytosine 10, which adopts two conformations in the crystal (only
one conformation is shown).