journal menu
![[Figure 1]](ud5045fig1mag.jpg)
|
|
Figure 1
(a) SDS–PAGE and Western blot analysis of baculovirus-expressed PvS1FL-bac (lane 1) and Drosophila S2 cell-expressed PvS1FL (lane 2) and PvS1FL-ng (lane 3). Left panel: Coomassie Blue staining. Middle panel: Western blotting with anti-His-tag antibodies. Right panel: Western blotting with anti-PvS1 antibodies (Bouillon et al., 2013  ). Protein molecular weights (MW) are indicated in kDa. (b) Scheme of full-length PvS1 composed of the prodomain (belt domain in yellow and classical subtilase prodomain in green) and catalytic domain (blue) with the boundary residues indicated and the four catalytic residues (Asp316, His376, Asn464 and Ser549) that define PvS1 as a subtilase. Dotted lines represent unstructured segments that are not visible in the crystal structure of the full-length protein (Giganti et al., 2014). Red bars indicate the locations of the three potential N-glycosylation sites (Asn361, Asn432 and Asn445) that are mutated to serines in PvS1FL-ng. Lower panels, the two constructs crystallized in this work; the different proteolytic cleavage sites discussed in the text are indicated by vertical arrows. Residue numbering refers to the native Plasmodium vivax subtilisin-like 1 serine protease (GenBank accession No. FJ536584). |
![[Figure 1]](ud5045fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
