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1.
Fig. 1

Fig. 1. The substrate specificity of 3-OST isoforms and the biological functions of the HS modified by different 3-OST isoforms. From: Engineering Sulfotransferases to Modify Heparan Sulfate.

Different 3-OST isoforms transfer a sulfo group (SO3) to the 3-OH position of glucosamine present in different disaccharide units. 3-OST-1-like activity transfers a sulfo group to the glucosamine residue that is either linked to the glucuronic acid (GlcUA) or the iduronic acid (IdoUA), yielding the product containing disaccharides −GlcUA-GlcNS3S±6S- or −IdoUA-GlcNS3S±6S-. HS modified by 3-OST-1 binds to antithrombin and has the anticoagulant activity. The 3-OST-3-like activity transfers a sulfo group to the glucosamine residue that is linked to the 2-O-sulfated iduronic acid (IdoUA2S) to yield the product containing the disaccharide of −IdoUA2S-GlcNR±3S6S- (R = −H or −SO3). HS modified by 3-OST-3 binds to herpes simplex virus type 1 gD and serves as an entry receptor for herpes simplex virus type 1. 3-OST-5 has both 3-OST-1-like and 3-OST-3-like activities, thus, the HS modified by 3-OST-5 binds to both antithrombin and gD and has both the anticoagulant activity and serves as an entry receptor for herpes simplex virus.

Ding Xu, et al. Nat Chem Biol. ;4(3):200-202.
2.
Fig. 2

Fig. 2. Structural characterization of 3-O-sulfotransferase isoforms 1, 3, and 5. From: Engineering Sulfotransferases to Modify Heparan Sulfate.

A. Ribbon diagram of the crystal structure of human 3-OST-5 with bound PAP (5). Secondary structural elements are shown as α-helices (blue, labeled as A#), β-strands (green, labeled as B#), and random coils (yellow). The bound PAP molecule is drawn as ball-and-stick (cyan). This figure was created using Molscript and Raster3D. Panels B–D show substrate recognition by 3-OST enzymes via a gating structure. The bound PAP molecule is shown as ball-and-stick, though only the phosphate moieties (orange) are visible due to their buried location. Amino acid residues are shown on the surface in red, and are labeled in white text. Distances measured are shown as black dotted lines, and are labeled in white. The position of the substrate binding cleft is shown as a dashed green arrow. B. Key amino acid residues forming a ‘gate’ on the nonreducing end of the substrate binding cleft of m3-OST-1. C. Structurally corresponding gate residues in h3-OST-3. The bound tetrasaccharide substrate (ΔUA2S-GlcNS6S-IdoUA2S-GlcNS6S, 6) is drawn as ball-and-stick, with the glucosamine residue to be sulfated circled in yellow. D. Structurally corresponding gate residues in h3-OST-5. These molecular surfaces were generated using PyMOL.

Ding Xu, et al. Nat Chem Biol. ;4(3):200-202.

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