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![[Figure 1]](yt5103fig1mag.jpg)
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Figure 1
Crystal structure of J30 as a cartoon representation with (a) and without (b) the protein surface. J30 wt contains an N-terminal Ig-like domain and a C-terminal catalytic domain, as is common among GH family 9 members. The side chains of the catalytic amino-acid residues Asp147 and Glu523 are depicted in teal. Also highlighted are the side chains corresponding to the residues mediating Zn2+ coordination in the triple mutant J30 CCH. (a) Residues Asp147 and Glu523 are positioned at the active site and in the center of the substrate-binding channel. (b) The active site (red asterisk) and Zn2+-introduction site (purple asterisk) are separate sites in proximity to one another. Within the catalytic domain, the (α/α)6-barrel structure (bottom left) and the four-stranded β-sheet (bottom right) are turned into perspective. |
![[Figure 1]](yt5103fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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