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PDBsum entry 2nog
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DNA binding protein
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PDB id
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2nog
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References listed in PDB file
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Key reference
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Title
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Structure of the sant domain from the xenopus chromatin remodeling factor iswi.
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Authors
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J.R.Horton,
S.J.Elgar,
S.I.Khan,
X.Zhang,
P.A.Wade,
X.Cheng.
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Ref.
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Proteins, 2007,
67,
1198-1202.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 2.
Figure 2. Structure of Xenopus SANT. (A) A dimer of SANT domain
formed in the crystallographic asymmetric unit. The dimer
interface is formed between the N-terminal Pro-rich
loop--hydrophobic interactions involving proline residues (P743,
P746, P748, and P749) and helix  A
(Tyr775 and Tyr781) - and the helix D
(two salt bridges between invariant Arg803 of one protomer and
invariant Asp804 of another protomer). The Stokes radius of the
domain was consistent with a solution dimer: the 21-kDa protein
eluted from S75 gel filtration column with apparent molecular
weight of 41 kDa. The total area of dimer interface of 707
Å^2 is within the limits, though at the lower end, of the
32 homodimers examined.[9] (B) A 90° rotated view from panel
A. A Mg^2+ ion, required for crystallization, is bound at the
loop region between helices E
and F.
Three main chain carbonyl oxygen atoms of Ala852, Val855, and
Lys858 and two water molecules (w) coordinate the metal atom.
(C) GRASP surface charge distribution is displayed with blue for
positive, red for negative, and white for neutral. Filled circle
indicates the opening of the concave L-surface. (D) Three views
of the monomer structure of Xenopus SANT domain.
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Figure 3.
Figure 3. Structural comparisons. (A) Xenopus and Drosophila
SANT domains are colored in green and grey, respectively. The
additional N-terminal helix in the Drosophila protein is in red,
and the C-terminal SLIDE domain is shaded in yellow. The
proteolytic cleavage site in the Xenopus protein is indicated.
(B) Xenopus SANT domain and cMyb R2R3 are colored in green and
magenta, respectively (middle panel). Structural alignment of
helices D,
E,
and F
of Xenopus SANT and that of R2 of c-Myb R2R3 (PDB 1GV2) derived
the superimposition. The left panel shows the acidic surface
patch of Xenopus SANT and the right panel shows the
corresponding region of basic DNA binding surface of R2 of c-Myb
R2R3. (C) X-ray structure of c-Myb R2R3[11] with the locations
of three hydrophobic residues whose mutation to polar or charged
side chains affecting the ability of v-Myb interaction with
histone (left panel). A surface groove on the opposite side of
the DNA binding might be the binding groove for histone H3
peptide.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
67,
1198-1202)
copyright 2007.
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