Figure 4 - full size

 

Figure 4.
Topology diagram of the TPP1 structure showing the prosegment (Ser^20-Ser^180) and the catalytic domain (His^197-Pro^563).α-Helices are labeled α and are represented by cylinders, and β-strands are labeled β and represented by arrows. Residues that are involved in the catalytic mechanism are marked by red letters; the 6 cysteine residues that form disulfide bridges are colored yellow on black background, and the asparagine residues that carry N-linked oligosaccharides are highlighted by a turquoise background. No density could be observed for a possible glycosylation at Asn^222 (highlighted with gray background). The linker region (Ser^181-Leu^196) was poorly defined (gray letters). The first amino acid R of the purification tag RSHHHHHH is displayed in gray.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2009, 284, 3976-3984) copyright 2009.