Fig. 5: The EXTL3 GT47 domain adopts a GT-B fold but appears to lack an appropriate nucleotide sugar binding pocket. | Nature Communications

Fig. 5: The EXTL3 GT47 domain adopts a GT-B fold but appears to lack an appropriate nucleotide sugar binding pocket.

From: The structure of EXTL3 helps to explain the different roles of bi-domain exostosins in heparan sulfate synthesis

Fig. 5

a EXTL3 GT47 domain (from one individual chain). Strands in the central sheets are coloured purple to yellow in order of most N-terminal to most C-terminal. b Secondary structure schematic of a generic GT-B-fold glycosyltransferase. c Secondary structure schematic of EXTL3 GT47 domain, showing correspondence of the central strands to the GT-B archetype. d Structural alignment of the EXTL3 GT47 domain to the closest four GT-B matches from PDB25 identified using DALI (omitting duplicate family members). Left: C-terminal subdomain of EXTL3 GT47 domain (focussing on the Cα3 and Cα4 helices); right: hits from DALI without EXTL3 (only Cα3–Cα4 portion shown for clarity); centre: merged. Structures, by PDB accession and GT family, from highest to lowest match are: 5F84 (GT90; pale blue), 1IXY (GT63; purple), 4W6Q (GT113; pale green), 6EJI (GT4; orange). e Protein sequence alignment of EXTL3 GT47 domain with other GT47 domain-containing proteins from Homo sapiens and Arabidopsis thaliana (only the Cα3–Cα4 portion is shown for brevity). Arg421 and Glu453 residues from EXTL3, as well as their analogues in other GT47 sequences, are highlighted in bold; the positions of the Cα3 and Cα4 helices in the EXTL3 sequence are highlighted in pale grey.

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