5T05
Crystal structure of heparan sulfate 6-O-sulfotransferase with bound PAP and IdoA2S containing hexasaccharide substrate
Summary for 5T05
| Entry DOI | 10.2210/pdb5t05/pdb |
| Related | 5T03 5T0A |
| Related PRD ID | PRD_900010 |
| Descriptor | maltose binding protein - heparan sulfate 6-O-sulfotransferase isoform 3 fusion protein, 2-deoxy-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid-(1-4)-2-deoxy-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | heparan sulfate, sulfotransferase, complex, transferase |
| Biological source | Escherichia coli O157:H7 More |
| Total number of polymer chains | 2 |
| Total formula weight | 164114.51 |
| Authors | Pedersen, L.C.,Moon, A.F.,krahn, J.M.,Liu, J. (deposition date: 2016-08-15, release date: 2017-02-01, Last modification date: 2024-11-13) |
| Primary citation | Xu, Y.,Moon, A.F.,Xu, S.,Krahn, J.M.,Liu, J.,Pedersen, L.C. Structure Based Substrate Specificity Analysis of Heparan Sulfate 6-O-Sulfotransferases. ACS Chem. Biol., 12:73-82, 2017 Cited by PubMed Abstract: Heparan sulfate (HS) is a sulfated polysaccharide exhibiting essential physiological functions. HS 6-O-sulfotransferase (6-OST) transfers a sulfo group to the 6-OH position of glucosamine units to confer a variety of HS biological activities. There are three different isoforms of 6-OST in the human genome. Here, we report crystal structures of the ternary complex of 6-OST with the sulfo donor analog 3'-phosphoadenosine 5'-phosphate and three different oligosaccharide substrates at 1.95 to 2.1 Å resolutions. Structural and mutational analyses reveal amino acid residues that contribute to catalysis and substrate recognition of 6-OST. Unexpectedly, the structures reveal 6-OST engages HS in a completely different orientation than other HS sulfotransferases and sheds light on the basic HS requirements for specificity. These findings also contribute structural information to understand mutations in human 6-OST isoform 1 associated with the human genetic disease idiopathic hypogonadotropic hypogonadism characterized by incomplete or lack of puberty. PubMed: 28103688DOI: 10.1021/acschembio.6b00841 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.952 Å) |
Structure validation
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