ISDA: 11OS

Deposition Date 2026-03-06

Release Date 2026-09-23

Last Version Date 2026-09-23

Entry Detail

PDB ID:

11OS

Keywords:

PROTEIN BINDING

Title:

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

Biological Source:

Source Organism(s):

Mattirolomyces terfezioides (Taxon ID: 74857)

Expression System(s):

Komagataella phaffii

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.23 Å

R-Value Free:

0.16

R-Value Work:

0.13

R-Value Observed:

0.13

Space Group:

P 21 21 21

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Macromolecular Entities

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Honey Truffle Active Componen
Chain IDs:A, B
Chain Length:0
Number of Molecules:2
Biological Source:Mattirolomyces terfezioides

Ligand Molecules

P6G

Primary Citation

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

Pitkanen, T.T, Cooper, A, Vo, P, McFarland, C.T, Patnaik, R, Lovell, S, Connors, D.E.Show

Acta Crystallogr.,Sect.F ? ? ? (2026)

PMID: 42742198 DOI: 10.1107/S2053230X26008745

Abstact

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 P2(1)2(1)2(1)) and monoclinic (space group P2(1)) crystal structures of HT-AC are reported at resolutions ranging from 1.23 to 1.70 A.

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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