11OX
Crystal Structure of Honey Truffle Active Component 1 through 4 with glucose bound (Monoclinic P form)
Summary for 11OX
| Entry DOI | 10.2210/pdb11ox/pdb |
| Descriptor | Honey Truffle Active Component 1 through 4, CHLORIDE ION, beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | honey truffle active component 1 through 4, sweet tasting protein, protein binding |
| Biological source | Mattirolomyces terfezioides |
| Total number of polymer chains | 2 |
| Total formula weight | 27003.73 |
| Authors | Lovell, S.,Cooper, A.,Connors, D.E.,Pitkanen, T.T.,McFarland, C.T.,Vo, P.,Patnaik, R. (deposition date: 2026-03-06, release date: 2026-09-23) |
| Primary citation | Pitkanen, T.T.,Cooper, A.,Vo, P.,McFarland, C.T.,Patnaik, R.,Lovell, S.,Connors, D.E. Crystal structures of the sweet-tasting protein honey truffle active component from Mattirolomyces terfezioides. Acta Crystallogr.,Sect.F, 2026 Cited by PubMed Abstract: Crystal structures of honey truffle active component (HT-AC) originally derived from the fungus Mattirolomyces terfezioides are reported for the first time. HT-AC is a 13 kDa protein and is one of a small class of unrelated proteins that interact with an allosteric site on the human T1R2/R3 sweet taste receptor. These proteins can be used as sweeteners, and result in sweet taste perception at lower concentrations than sugar (the orthosteric receptor target) or many other high-intensity small-molecule sweeteners. Orthorhombic (space group P222) and monoclinic (space group P2) crystal structures of HT-AC are reported at resolutions ranging from 1.23 to 1.70 Å. PubMed: 42742198DOI: 10.1107/S2053230X26008745 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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