journal menu
![[Figure 3]](jc5051fig3mag.jpg)
|
|
Figure 3
The structure of CbpD reveals that some chitin-specific motifs are preserved while others are more similar to cellulose-specific motifs. (a) The active site of CbpD contains a canonical His-brace motif. 2Fo − Fc electron density contoured at 0.7σ allows copper to be modeled into the active site (sphere_scale 0.6), approximately 2 Å away from the three coordinating N atoms, as expected. (b) The CbpD active site also contains a number of highly conserved residues. (c) Motifs previously identified as conserved among and/or proposed to confer substrate specificity in chitin- and cellulose-active LPMOAA10s are mapped to sequence logos generated from multiple sequence alignments of 13 chitin-active and seven cellulose-active LPMOAA10s listed as experimentally validated in the CAZy database (Drula et al., 2022  ) and in Zhou & Zhu (2020), with the addition of CbpD to the chitin-active sequences. Motifs were concatenated for display and residues are numbered as in CbpD for the chitin-active sequence logo. In the cellulose-active sequence logo, residues are numbered by the structurally equivalent position in CbpD. The CbpD amino-acid identities are below the chitin logo. MSAs were generated with the T-Coffee web server (Notredame et al., 2000; Di Tommaso et al., 2011). Sequence logos were generated with WebLogo (Crooks et al., 2004). |
![[Figure 3]](jc5051fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
