journal menu
![[Figure 1]](wa5073fig1mag.jpg)
|
|
Figure 1
(a) Domain structure of full-length Cwp84. The domains are indicated as follows: signal peptide, grey; propeptide, red; cysteine protease, green; lectin-like, cyan; CWBDs, purple. Active-site residues are indicated in pink, while calcium ion-coordinating residues are shown in orange. The region crystallized, consisting of residues 33–497, is bracketed below. (b) Ribbon diagram of the three-dimensional structure of the propeptide, cysteine protease and lectin-like domains. The domains are coloured according to (a) and the calcium ion is represented as an orange sphere. The disordered region between Lys81 and Tyr89 can be observed as a discontinuity in the ribbon at the bottom centre of the image. (c) Molecular surface of Cwp8433–497. The close interaction of the propeptide with the cysteine protease and lectin-like domains is shown, particularly at the active site formed at the interface between the cysteine protease and lectin-like domains. The domains are coloured according to (a). |
![[Figure 1]](wa5073fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
