3BD9
human 3-O-sulfotransferase isoform 5 with bound PAP
Summary for 3BD9
Entry DOI | 10.2210/pdb3bd9/pdb |
Descriptor | Heparan sulfate glucosamine 3-O-sulfotransferase 5, ADENOSINE-3'-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | 3-o-sulfotransferase, heparan sulfate, heparan sulfate biosynthesis, substrate specificity, glycoprotein, golgi apparatus, membrane, signal-anchor, transmembrane, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Golgi apparatus membrane; Single-pass type II membrane protein (Probable): Q8IZT8 |
Total number of polymer chains | 1 |
Total formula weight | 33396.25 |
Authors | Xu, D.,Moon, A.F.,Song, D.,Liu, J.,Pedersen, L.C. (deposition date: 2007-11-14, release date: 2008-01-29, Last modification date: 2024-10-09) |
Primary citation | Xu, D.,Moon, A.F.,Song, D.,Pedersen, L.C.,Liu, J. Engineering sulfotransferases to modify heparan sulfate. Nat.Chem.Biol., 4:200-202, 2008 Cited by PubMed Abstract: The biosynthesis of heparan sulfate (HS) involves an array of specialized sulfotransferases. Here, we present a study aimed at engineering the substrate specificity of different HS 3-O-sulfotransferase isoforms. Based on the crystal structures, we identified a pair of amino acid residues responsible for selecting the substrates. Mutations of these residues altered the substrate specificities. Our results demonstrate the feasibility of tailoring the specificity of sulfotransferases to modify HS with desired functions. PubMed: 18223645DOI: 10.1038/nchembio.66 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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