11OS

Crystal Structure of Honey Truffle Active Component 1 through 4 (Orthorhombic P form)

Summary for 11OS

• Entry DOI: 10.2210/pdb11os/pdb
• Descriptor: Honey Truffle Active Component 1 through 4, CHLORIDE ION, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: honey truffle active component 1 through 4, sweet tasting protein, mattirolomyces terfezioide, protein binding
• Biological source: Mattirolomyces terfezioides
• Total number of polymer chains: 2
• Total formula weight: 27141.36

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

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: 42742198
DOI: 10.1107/S2053230X26008745

Experimental method

X-RAY DIFFRACTION (1.23 Å)