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Review
. 2010 Jun;153(2):444-55.
doi: 10.1104/pp.110.156646. Epub 2010 Apr 20.

The biochemistry and structural biology of plant cell wall deconstruction

Harry J Gilbert  1
Affiliations
Review

The biochemistry and structural biology of plant cell wall deconstruction

Harry J Gilbert. Plant Physiol. 2010 Jun.
No abstract available

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Figures

Figure 1.
Figure 1.
Structural convergence and divergence in plant cell wall hydrolases. In the examples shown, a GH28 polygalacturonase (green; Protein Data Bank [PDB] no. 1BHE) and GH49 dextranase (pink; PDB 1OGM) are the clan GH-N representative enzymes. The clan GH-C enzymes are a GH11 xylanase (green; PDB 1BCX) and a GH12 endoglucanase (light blue; PDB 1OA4). The clan GH-A enzymes are a GH5 endoglucanase (magenta; PDB 1A3H), GH26 mannanase (blue; PDB 2BVT), and a GH53 endo-β-1,4-galactanase (green; PDB 1R8L). The catalytic residues are shown in stick format in a darker form of the respective color of the protein fold. Convergent evolution is evident by the observation that xylanases are found in three glycoside hydrolase families that display very different folds.
Figure 2.
Figure 2.
An overlay of an endo (CjMan26A; green) and an exo (CjMan26C; cyan) β-mannanase from Cellvibrio japonicas. A small extension of the loop at the distal −2 subsite presents two residues, Asp-130 and Leu-129, shown in stick format in purple. These residues present a steric block that prevents extension of substrate distal to the sugar bound at the −2 subsite. The residues shown in dark blue, in the surface representations of the two enzymes, are Asp-130 in CjMan26C and the equivalent amino acid (Glu-121) in CjMan26A.
Figure 3.
Figure 3.
Examples of type A, type B, and type C CBMs. CBM2a is derived from the Cellulomonas fimi xylanase Xyn10A (Protein Data Bank [PDB] 1XG), CBM15 is a component of the C. japonicas xylanase Xyn10C (PDB 1GNY), and CBM9 is from a Thermotoga maritima GH10 xylanase (PDB 1I82). The folds are ramped from blue (N terminus) to red (C terminus). The three aromatic residues that form a ligand-binding apolar surface in the CBM2a module are colored red and are shown in stick format in the respective surface and fold depictions of the protein.
Figure 4.
Figure 4.
The structural features of the active site of CtCE2 that displays esterase and a CBM function. The catalytic module of CtCE2 contains two discrete domains that display a typical α/β-hydrolase fold (blue), evident in Ser esterases, and a jelly roll fold (red), respectively. The surface representation of CtCE2 reveals a cleft that accommodates cellopentaose (shown in yellow) and houses the active site of the esterase. The three aromatic residues that play a key role in binding cellulose are shown in red. The active site of three CE2 esterases show cellopentaose (gray) and the three aromatic residues (green) from CtCE2, the two aromatic residues (magenta) in CjCE2B, and the single aromatic amino acid (yellow) in CjCE2A. All three enzymes are Ser esterases, and the catalytic triad (Ser-160, His-335, Asp-333) of CE2A is displayed in yellow.
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