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Figure 3.
Fig. 3. Tertiary structure of SUMO-2 and comparison with
other proteins.(A) A ribbon representation of the protein fold.
(B) A topology diagram with well-defined backbone hydrogen
bonds. The helices (  1, 2) and strands
(  1– 5) are
coloured in magenta, blue, green, yellow and red from N to C
terminus. The hydrogen bond distances, with a criterion of less
than 3.2 Å, are observed in the refined model at 1.2
Å, with one exception between Asp16 and Arg36, which is
seen in the 1.6 Å model. The amino acids are shaded in
red, green and blue for acidic, neutral and basic polar
residues, and in yellow for prolines and glycines. In (C) the
polypeptide tracings of two SUMO-2 models from type I (12–89)
and type II (17–88) crystals, shown in green and red, are
superimposed with that of human ubiquitin (1–76), shown in
blue. In (D) the yeast SMT3 crystal structure (20–98) and
human SUMO-1 NMR structure (–2–101), coloured yellow and
cyan, respectively, are compared with the SUMO-2 structure (type
I crystal), shown in red.
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