A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
Figure 5
Conservation of carbohydrate-binding residues in the galactose-binding-like domain of M17 homologues of Entamoeba.
A. The domain architecture of M17 (EHI_015380). The transmembrane domain and the galactose binding-like domain (IPR008979) were identified using Philius [66] and InterProScan software packages, respectively. B. The amino acid sequence alignment of the carbohydrate-binding domain of M17 homologues in Entamoeba and GH84C of C. perfringens (PBD ID: 2V5D_A). Residues with >75% identity are highlighted. M17 homologues of E. dispar (prefix EDI) and E. invadens (prefix EIN) were identified using BLASTP analysis of their proteomes, with M17 as the query. The arrows indicate the carbohydrate binding residues in GH84C [62]. C. Predicted structural model of the galactose-binding like domain of M17. The model was predicted from the 3D jury meta-server [67], with C. perfringens GH84C as the best-hit template (i.e. the template with the highest 3D-jury score = 81.56; score of 50 is the default cut-off, which results in a prediction accuracy of above 90%). The side-chains of the three conserved carbohydrate binding residues are coloured and labelled as in panel B.