Tyler T. Pitkanen, Anne Cooper, Phillip Vo, Chase T. McFarland, Ranjan Patnaik, Scott Lovell, Daniel E. Connors
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引用次数: 0
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.
期刊介绍:
Acta Crystallographica Section F is a rapid structural biology communications journal.
Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal.
The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles.
Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.