Figure 1 | Scientific Reports

Figure 1

From: Structural and functional role of disulphide bonds and substrate binding residues of the human beta-galactoside alpha-2,3-sialyltransferase 1 (hST3Gal1)

Figure 1

A view of the active site of human and porcine ST3Gal1 enzymes. (A) Cartoon representation of pST3Gal1 (PDB 2wnb). Positions previously mutated in pST3Gal112 and hST3Gal123 are shown as white sticks and as blue outlines, respectively. In the latter enzyme, only H316 and H299 are part of the active/binding site. Amino acid sequence numbering for porcine and human enzymes is in green and black font, respectively. (B) Cartoon representation of modelled hST3Gal1. Positions selected for mutagenesis of hST3Gal1 in this paper are displayed as blue sticks. CMP and acceptor Gal-β-1,3-GalNAc-α-PhNO2 from pST3Gal1 (PDB 2wnb, green sticks) as well as CMP3F-Neu5Ac from the sialyltransferase CstII of Campylobacter jejuni (PDB 1ro7, orange sticks) are shown in the active site. Possible interactions between binding site residues and substrates (<4 Å) are displayed as dashed lines. Disulphide bonds are located >16 Å away from donor and acceptor binding sites. Structures of CstII and pST3Gal1 as well as the model of hST3Gal1 were aligned with UCSF Chimera (http://www.rbvi.ucsf.edu/chimera).

Back to article page