3aok
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of sweet-tasting protein thaumatin II== | |
| + | <StructureSection load='3aok' size='340' side='right'caption='[[3aok]], [[Resolution|resolution]] 1.27Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3aok]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AOK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aok OCA], [https://pdbe.org/3aok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aok RCSB], [https://www.ebi.ac.uk/pdbsum/3aok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aok ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/THM2_THADA THM2_THADA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thaumatin, an intensely sweet-tasting protein, elicits a sweet taste sensation at 50nM. Here the X-ray crystallographic structure of one of its variants, thaumatin II, was determined at a resolution of 1.27A. Overall structure of thaumatin II is similar to thaumatin I, but a slight shift of the Calpha atom of G96 in thaumatin II was observed. Furthermore, the side chain of residue 67 in thaumatin II is highly disordered. Since residue 67 is one of two residues critical to the sweetness of thaumatin, the present results suggested that the critical positive charges at positions 67 and 82 are disordered and the flexibility and fluctuation of these side chains would be suitable for interaction of thaumatin molecules with sweet receptors. | ||
| - | + | Crystal structure of the sweet-tasting protein thaumatin II at 1.27A.,Masuda T, Ohta K, Tani F, Mikami B, Kitabatake N Biochem Biophys Res Commun. 2011 Jul 8;410(3):457-60. Epub 2011 Jun 6. PMID:21672520<ref>PMID:21672520</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3aok" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thaumatococcus daniellii]] | ||
| + | [[Category: Kitabatake N]] | ||
| + | [[Category: Masuda T]] | ||
| + | [[Category: Mikami B]] | ||
Current revision
Crystal structure of sweet-tasting protein thaumatin II
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