9EP0
Dolichyl phosphate mannose synthase in complex with donor (GDP-Man) and traces of acceptor (Dol55P) and product (Dol55P-Man)
Summary for 9EP0
| Entry DOI | 10.2210/pdb9ep0/pdb |
| Descriptor | Dolichol monophosphate mannose synthase, GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | dolichyl phosphate mannose synthase, enzyme, integral membrane protein, protein glycosylation, glycosylphosphatidylinositol synthesis, gdp-mannose, dolichyl monophosphate, dolichol monophosphate mannose, donor-acceptor and product complex, transferase |
| Biological source | Pyrococcus furiosus DSM 3638 |
| Total number of polymer chains | 1 |
| Total formula weight | 44451.94 |
| Authors | Gandini, R.,Keskitalo, M.M.,Reichenbach, T.,Divne, C. (deposition date: 2024-03-16, release date: 2025-10-01, Last modification date: 2026-04-15) |
| Primary citation | Gandini, R.,Keskitalo, M.M.,Reichenbach, T.,Kalyani, D.C.,Divne, C. Crystallographic data for Pyrococcus furiosus dolichylphosphate mannose synthase suggest that the enzyme could flip its glycolipid product. Sci Rep, 16:-, 2026 Cited by PubMed Abstract: Dolichylphosphate mannose synthase (DPMS) performs an essential function by synthesizing the activated lipid-linked mannose intermediate used in protein glycosylation pathways. In eukaryotes and archaea, DPMS catalyzes the transfer of mannose from GDP-mannose to dolichylphosphate to generate dolichylphosphate mannose (Dol-P-Man). Type-III DPMS from Pyrococcus furiosus (PfDPMS) has a catalytic domain attached to a GtrA-like transmembrane (TM) domain with an unusual topology. Here, we present crystallographic data from a crystal complex determined from an enzymatic reaction mixture that provides detailed information about donor- and acceptor binding in the active site prior to mannosyl transfer. We also present a new, unexpected structural state for the TM domain in which a Dol-P-Man molecule is bound "upside-down" with its mannosylphosphate headgroup positioned in a polar pocket between the TM helices. By generating a panel of TM-domain mutants, we confirm that the TM domain does not participate directly in the catalysis of mannosyl transfer and discuss the possibility of this domain providing moonlighting function to PfDPMS by translocating the Dol-P-Man product to the cell exterior. PubMed: 41826688DOI: 10.1038/s41598-026-44343-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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