Purification and Functional Characterisation of Rhiminopeptidase A, a Novel Aminopeptidase from the Venom of Bitis gabonica rhinoceros
Figure 5
The modelled structure of rhiminopeptidase A.
MODELLER was used to create a model of the structure of rhiminopeptidase A using the determined structure of tricorn interacting factor F3 from T. acidophilum (PDB code 1z5h) as a template. A, image of the 4-domain structure of rhiminopeptidase A with the domains coloured as follows: N-terminal saddle shaped β-sheet domain in red; catalytic domain in orange; β-sandwich domain in yellow and C-terminal α-helical domain in green. Key functional residues are highlighted as follows: zinc ligands in blue, calcium binding site in cyan, substrate binding residues in grey and the threonine involved in substrate specificity in magenta. B, detailed view of the key functional residues coloured as in A. The images were generated using PyMOL.