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Figure 1.
Structure of the Eaf3 chromo domain. A, overall structure and
electrostatic surface of the short form Eaf3 chromo domain
(residues 1–113). B, overall structure and electrostatic
surface of the long form Eaf3 chromo domain (residues 1–124).
The C-terminal part forms a stable α-helix in both structures.
The Eaf3 chromo domain contains a 38-residue insertion (shown in
red), which, together with the β-barrel core, forms a long,
deep surface groove. C, sequence comparison of the chromo domain
from yeast Eaf3, human MRG15, and Drosophila HP1. Strictly
conserved residues are highlighted in shaded red boxes, and
conserved residues are highlighted in open red boxes. The
secondary structure of the Eaf3 chromo domain is placed above
the alignment. D, structural comparison of the Eaf3 chromo
domain (cyan, insertion in red) with the MRG15 (gray, Protein
Data Bank code 2F5K) and HP1 (purple, Protein Data Bank code
1KNA) chromo domains. Residues forming the hydrophobic pocket
are shown with side chains. The bound peptide in the HP1 chromo
domain complex is shown in magenta.
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