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![[Figure 3]](ud5045fig3mag.jpg)
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Figure 3
(a) Limited proteolysis of PvS1Cat with trypsin, subtilisin A, chymotrypsin and papain. Samples were taken at different time points and analysed by SDS–PAGE followed by Coomassie Blue staining. (b) Coomassie Blue staining and Western blotting using anti-His antibodies of purified PvS1Cat-Tryps. Protein molecular weights are indicated in kDa. (c) Superposition of the size-exclusion chromatography profiles of PvS1FL-ng, PvS1Cat and PvS1Cat-Tryps on a Superdex 75 16/60 column. (d) Crystal structure of PvS1Cat-Tryps showing the two polypeptide chains (blue and grey) that are present in the asymmetric unit. Active-site residues (Asp316, His372 and Ser549) are shown in red and solvent-exposed empty catalytic grooves are indicated by arrows. (e) Structural alignment of PvS1FL-bac (PDB entry 4tr2, residues Tyr277–Lys611, cyan) and PvS1Cat-Tryps (magenta) catalytic grooves. |
![[Figure 3]](ud5045fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
