3e3s
Structure of thaumatin with the magic triangle I3CStructure of thaumatin with the magic triangle I3C
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedObtaining phase information for the solution of macromolecular structures is still one of the bottlenecks in X-ray crystallography. 5-Amino-2,4,6-triiodoisophthalic acid (I3C), in which three covalently bound iodines form an equilateral triangle, was incorporated into proteins in order to obtain phases by single-wavelength anomalous dispersion (SAD). An improved binding capability compared with simple heavy-metal ions, ready availability, improved recognition of potential heavy-atom sites and low toxicity make I3C particularly suitable for experimental phasing. A magic triangle for experimental phasing of macromolecules.,Beck T, Krasauskas A, Gruene T, Sheldrick GM Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1179-82. Epub 2008, Oct 18. PMID:19020357[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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