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![[Figure 4]](jc5049fig4mag.jpg)
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Figure 4
The structure of MtGlu5 in comparison with those of TmCel5A and CBM29-2. (a) Superimposition of the active-site residues in the catalytic pocket of MtGlu5 (dark blue) on the corresponding site of TmCel5A in complex with cellotetraose and glucose (blue/white; PDB entries 3azt and 3azr), depicted in stick representation, reveals the conservation of amino-acid residues between MtGlu5 and TmCel5A. Likewise, in an overlay of the structure of MtCBM (dark blue) and CBM29-2 in complex with cellohexaose (yellow; PDB entry 1w8t), with the three conserved aromatic residues shown in stick format, reveals substrate binding by MtCBM in a similar way to CBM29-2 (c). (b) A putative binding groove of MtGlu5 with many Trp residues on the solvent-exposed hydrophobic surface: Trp43, Trp188, Trp192, Trp224, Trp249, Trp251 and Trp270 are shown together with Glu216 for comparison. |
![[Figure 4]](jc5049fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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