Figure 5.
FIG. 5. Comparison of the 174 loop and 99 loop in AaV-SP-I
(cyan) AaV-SP-II (yellow), and TSV-PA (silver-gray) shows the
architectural features of substrate binding sites S2 S4 of the
three proteins. The key residues (215, 178, 173, 174, 97, 98,
99) for substrate-binding are shown with stick model. The
hydrogen bonds between Tyr215 and Glu173 of the two AaV-SPs and
the hydrogen bond between Glu97 and Tyr178 of AaV-SP-I are
shown. The amino acid residues of AaV-SPs and TSV-PA are
displayed in black and blue. The schematic substrate-binding
sites 2, 3, and 4 are indicated with a light green ellipse.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
10524-10529)
copyright 2005.
S4 of the
three proteins. The key residues (215, 178, 173, 174, 97, 98,
99) for substrate-binding are shown with stick model. The
hydrogen bonds between Tyr215 and Glu173 of the two AaV-SPs and
the hydrogen bond between Glu97 and Tyr178 of AaV-SP-I are
shown. The amino acid residues of AaV-SPs and TSV-PA are
displayed in black and blue. The schematic substrate-binding
sites 2, 3, and 4 are indicated with a light green ellipse.