5EKE
Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant)
Summary for 5EKE
| Entry DOI | 10.2210/pdb5eke/pdb |
| Related | 5EKP |
| Descriptor | Uncharacterized glycosyltransferase sll0501, URIDINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | glycosyltransferase, membrane protein, enzyme, bactoprenol, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, transferase |
| Biological source | Synechocystis sp. (strain PCC 6803 / Kazusa) |
| Total number of polymer chains | 4 |
| Total formula weight | 158687.21 |
| Authors | Ardiccioni, C.,Clarke, O.B.,Tomasek, D.,Banerjee, S.,Rajashankar, K.R.,Liu, Q.,Shapiro, L.,Mancia, F.,New York Consortium on Membrane Protein Structure (NYCOMPS) (deposition date: 2015-11-03, release date: 2016-01-06, Last modification date: 2024-03-06) |
| Primary citation | Ardiccioni, C.,Clarke, O.B.,Tomasek, D.,Issa, H.A.,von Alpen, D.C.,Pond, H.L.,Banerjee, S.,Rajashankar, K.R.,Liu, Q.,Guan, Z.,Li, C.,Kloss, B.,Bruni, R.,Kloppmann, E.,Rost, B.,Manzini, M.C.,Shapiro, L.,Mancia, F. Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun, 7:10175-10175, 2016 Cited by PubMed Abstract: The attachment of a sugar to a hydrophobic polyisoprenyl carrier is the first step for all extracellular glycosylation processes. The enzymes that perform these reactions, polyisoprenyl-glycosyltransferases (PI-GTs) include dolichol phosphate mannose synthase (DPMS), which generates the mannose donor for glycosylation in the endoplasmic reticulum. Here we report the 3.0 Å resolution crystal structure of GtrB, a glucose-specific PI-GT from Synechocystis, showing a tetramer in which each protomer contributes two helices to a membrane-spanning bundle. The active site is 15 Å from the membrane, raising the question of how water-soluble and membrane-embedded substrates are brought into apposition for catalysis. A conserved juxtamembrane domain harbours disease mutations, which compromised activity in GtrB in vitro and in human DPM1 tested in zebrafish. We hypothesize a role of this domain in shielding the polyisoprenyl-phosphate for transport to the active site. Our results reveal the basis of PI-GT function, and provide a potential molecular explanation for DPM1-related disease. PubMed: 26729507DOI: 10.1038/ncomms10175 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.001 Å) |
Structure validation
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