5yyr: Difference between revisions
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<StructureSection load='5yyr' size='340' side='right'caption='[[5yyr]], [[Resolution|resolution]] 1.07Å' scene=''> | <StructureSection load='5yyr' size='340' side='right'caption='[[5yyr]], [[Resolution|resolution]] 1.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yyr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YYR OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5yyr]] 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=5YYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YYR FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.07Å</td></tr> | ||
<tr id=' | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yyr OCA], [https://pdbe.org/5yyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yyr RCSB], [https://www.ebi.ac.uk/pdbsum/5yyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yyr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kigo | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Kitabatake | [[Category: Kigo S]] | ||
[[Category: Masuda | [[Category: Kitabatake N]] | ||
[[Category: Mikami | [[Category: Masuda T]] | ||
[[Category: Mitsumoto | [[Category: Mikami B]] | ||
[[Category: Ohta | [[Category: Mitsumoto M]] | ||
[[Category: Suzuki | [[Category: Ohta K]] | ||
[[Category: Tani | [[Category: Suzuki M]] | ||
[[Category: Tani F]] | |||
Latest revision as of 11:40, 22 November 2023
Structure K106A thaumatinStructure K106A thaumatin
Structural highlights
FunctionTHM1_THADA Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis. Publication Abstract from PubMedThaumatin, an intensely sweet-tasting protein, elicits sweet taste with a threshold of only 50 nM. Previous studies from our laboratory suggested that the complex model between the T1R2-T1R3 sweet receptor and thaumatin depends critically on the complementarity of electrostatic potentials. In order to further validate this model, we focused on three lysine residues (Lys78, Lys106, and Lys137), which were expected to be part of the interaction sites. Three thaumatin mutants (K78A, K106A, and K137A) were prepared and their threshold values of sweetness were examined. The results showed that the sweetness of K106A was reduced by about three times and those of K78A and K137A were reduced by about five times when compared to wild-type thaumatin. The three-dimensional structures of these mutants were also determined by X-ray crystallographic analyses at atomic resolutions. The overall structures of mutant proteins were similar to that of wild-type but the electrostatic potentials around the mutated sites became more negative. Since the three lysine residues are located in 20-40 A apart each other on the surface of thaumatin molecule, these results suggest the positive charges on the surface of thaumatin play a crucial role in the interaction with the sweet receptor, and are consistent with a large surface is required for interaction with the sweet receptor, as proposed by the multipoint interaction model named wedge model. Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.,Masuda T, Kigo S, Mitsumoto M, Ohta K, Suzuki M, Mikami B, Kitabatake N, Tani F Front Mol Biosci. 2018 Feb 13;5:10. doi: 10.3389/fmolb.2018.00010. eCollection, 2018. PMID:29487853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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