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Figure 5.
Fig. 5. Conformationalchange in tpe WpDloopmoves
Asp 356 into active site and3.6 A romnoxgen of
the boundsulfate.The unbound structure (residues 354-
358) is shown in lueand the sulfate-bound structure is
shown in yellow with red oxygens and blue nitrogens. The
peptide ond between Asp 356 andGln 357 lips between
thetwo formingatype 11 fi-turn in theclosed
conformation with Gln 57 at the i + 2 position.Thefol-
lowing is a list of , shifts between the two forms: Trp 354,
1.9 A; Pro 355,3.8 ; Asp356, 5.0 A; Gln 357, 6.7 A;
Thr 358,4.4 A.
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