2DPF
Crystal Structure of curculin1 homodimer
Summary for 2DPF
Entry DOI | 10.2210/pdb2dpf/pdb |
Descriptor | Curculin, SULFATE ION (3 entities in total) |
Functional Keywords | sweet taste, taste modifying, plant protein |
Biological source | Curculigo latifolia (lumbah) |
Total number of polymer chains | 4 |
Total formula weight | 51185.25 |
Authors | Kurimoto, E.,Suzuki, M.,Amemiya, E.,Yamaguchi, Y.,Nirasawa, S.,Shimba, N.,Xu, N.,Kashiwagi, T.,Kawai, M.,Suzuki, E.,Kato, K. (deposition date: 2006-05-11, release date: 2007-05-15, Last modification date: 2024-10-16) |
Primary citation | Kurimoto, E.,Suzuki, M.,Amemiya, E.,Yamaguchi, Y.,Nirasawa, S.,Shimba, N.,Xu, N.,Kashiwagi, T.,Kawai, M.,Suzuki, E.,Kato, K. Curculin Exhibits Sweet-tasting and Taste-modifying Activities through Its Distinct Molecular Surfaces. J.Biol.Chem., 282:33252-33256, 2007 Cited by PubMed Abstract: Curculin isolated from Curculigo latifolia, a plant grown in Malaysia, has an intriguing property of modifying sour taste into sweet taste. In addition to this taste-modifying activity, curculin itself elicits a sweet taste. Although these activities have been attributed to the heterodimeric isoform and not homodimers of curculin, the underlying mechanisms for the dual action of this protein have been largely unknown. To identify critical sites for these activities, we performed a mutational and structural study of recombinant curculin. Based on the comparison of crystal structures of curculin homo- and heterodimers, a series of mutants was designed and subjected to tasting assays. Mapping of amino acid residues on the three-dimensional structure according to their mutational effects revealed that the curculin heterodimer exhibits sweet-tasting and taste-modifying activities through its partially overlapping but distinct molecular surfaces. These findings suggest that the two activities of the curculin heterodimer are expressed through its two different modes of interactions with the T1R2-T1R3 heterodimeric sweet taste receptor. PubMed: 17895249DOI: 10.1074/jbc.C700174200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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