2dpf

From Proteopedia

Revision as of 14:29, 20 March 2008

Crystal Structure of curculin1 homodimer

Overview

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.

About this Structure

2DPF is a Single protein structure of sequence from Curculigo latifolia. Full crystallographic information is available from OCA.

Reference

Curculin exhibits sweet-tasting and taste-modifying activities through its distinct molecular surfaces., Kurimoto E, Suzuki M, Amemiya E, Yamaguchi Y, Nirasawa S, Shimba N, Xu N, Kashiwagi T, Kawai M, Suzuki E, Kato K, J Biol Chem. 2007 Nov 16;282(46):33252-6. Epub 2007 Sep 25. PMID:17895249

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