Crystal structures of the sweet-tasting protein honey truffle active component from Mattirolomyces terfezioides.

Authors

Tyler T Pitkanen, Anne Cooper, Phillip Vo, Chase T McFarland, Ranjan Patnaik, Scott Lovell, Daniel E Connors

Published in

Acta crystallographica. Section F, Structural biology communications. Oct 01, 2026. Epub Oct 01, 2026.

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 P2₁2₁2₁) and monoclinic (space group P2₁) crystal structures of HT-AC are reported at resolutions ranging from 1.23 to 1.70 Å.

PMID:
42742198
Bibliographic data and abstract were imported from PubMed on 15 Sep 2026.

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