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![[Figure 2]](ys5004fig2mag.jpg)
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Figure 2
(a) pH-dependent GlcNAc binding activity of FD1 at 277 K. The relative fractions, calculated as the eluted FD1 per total amount of protein applied to the GlcNAc column, are plotted against the pH (Tanio et al., 2007  ). The solid line is the regression curve, as calculated from equations (1) or (2) (see text). The calculation revealed that K1, K2, pKA, pKN and n are 0.41 ± 0.03, 1.94 ± 0.10, 6.06 ± 0.04, 6.30 ± 0.04 and 2.81 ± 0.46, respectively. The inset is the scheme of the equilibrium model proposed here. (b) Proposed conformational equilibrium between the active (slate) and non-active (magenta) forms of the P domain of FD1. In the active form the peptide bond between Asp282 and Cys283 is in the cis configuration. The putative model of the active conformation complexed with GlcNAc was built based on the crystal structure of tachylectin-5A complexed with GlcNAc (Kairies et al., 2001). |
![[Figure 2]](ys5004fig2.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
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