journal menu
![[Figure 1]](jc5049fig1mag.jpg)
|
|
Figure 1
A novel endoglucanase from M. taiwanensis WR220 with an inserted carbohydrate-binding module (CBM). (a) Molecular architecture of MtGlu5. The catalytic domain, which is shown in blue, belongs to glycoside hydrolase family 5, and the unique inserted CBM domain (orange) shares no homology with any other known GH5 sequence (Supplementary Fig. S1). (b) Structural overview of MtGlu5 (PDB entry 7vt8). Cartoon depicting the 3D structure of the catalytic domain (blue) with a (β/α)8 TIM-barrel fold; the novel inserted CBM (orange) presents a β-jelly-roll fold. (c) The molecular electrostatic surface of MtGlu5 in complex with a glucose molecule, which occupies the catalytic pocket. The glucose is sandwiched between the indole side chains of Trp43 and Trp224. The catalytic residues Glu149 and Glu393 are represented in stick format. (d) The amino-acid sequences of MtCBM and CBM29. The MtCBM sequence was aligned with CBM29 by ClustalW. The red triangles in the upper alignment indicate the conserved aromatic residues which are known to form the substrate-binding surface in CBM29; the red triangle in the lower alignment indicates the conserved glutamine residue for substrate recognition. (e) Overlap of MtCBM (dark blue; PDB entry 7vt8) with CBM29-2 (pale yellow; PDB entry 1w8t), showing that the overall fold is similar in MtCBM and CBM29-2. (f) The structure of MtCBM colour-ramped from the N-terminus (blue) to the C-terminus (red), with the three conserved Trp residues which are on the solvent-exposed surface shown in stick format. |
![[Figure 1]](jc5049fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
