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![[Figure 4]](dw5211fig4mag.jpg)
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Figure 4
Homology of MgGH51 to TxGH51. (a) Loop representation of the structure of MgGH51 superimposed with TxGH51. For MgGH51, the catalytic domain is shown in purple, the domain insertion in MgGH51 is shown in blue and the remodelled loops are shown in green. For TxGH51, the catalytic domain is shown in tan and the remodelled loops (or sites of loop insertion) are shown in red. The ligand bound to TxGH51 is shown in ball-and-stick representation. (b) Close-up view of the substrate-binding cleft of MgGH51 in surface representation with the same colouring as in (a). The L-arabinofuranose observed bound to MgGH51 is shown in purple and the three xylose residues observed in the TxGH51 structure are superposed onto the structure of MgGH51 to show the expected binding position of the xylan backbone. Phe354 and Phe441 are labelled and shown as sticks below the transparent surface. (c) Close-up view of the superimposed active sites of TxGH51 and MgGH51. Both enzymes are shown as cartoon representations with active-site residues and the bound L-arabinofuranose shown as ball-and-stick representations with the same colouring as in (a). Residue names are from MgGH51 unless marked with a star. The TxGH51 residue homologous to Glu351 was engineered to be Gln in place of the wild-type Glu. |
![[Figure 4]](dw5211fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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