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5x9m
From Proteopedia
(Difference between revisions)
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==Structure of hyper-sweet thaumatin (D21N)== | ==Structure of hyper-sweet thaumatin (D21N)== | ||
| - | <StructureSection load='5x9m' size='340' side='right' caption='[[5x9m]], [[Resolution|resolution]] 0.93Å' scene=''> | + | <StructureSection load='5x9m' size='340' side='right'caption='[[5x9m]], [[Resolution|resolution]] 0.93Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5x9m]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x9m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Katemfe Katemfe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9M FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9m OCA], [http://pdbe.org/5x9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9m RCSB], [http://www.ebi.ac.uk/pdbsum/5x9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9m ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9m OCA], [http://pdbe.org/5x9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9m RCSB], [http://www.ebi.ac.uk/pdbsum/5x9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | One of the sweetest proteins found in tropical fruits (with a threshold of 50nM), thaumatin, is also used commercially as a sweetener. Our previous study successfully produced the sweetest thaumatin mutant (D21N), designated hyper-sweet thaumatin, which decreases the sweetness threshold to 31nM. To investigate why the D21N mutant is sweeter than wild-type thaumatin, we compared the structure of the D21N mutant solved at a subatomic resolution of 0.93A with that of wild-type thaumatin determined at 0.90A. Although the overall structure of the D21N mutant resembles that of wild-type thaumatin, our subatomic resolution analysis successfully assigned and discriminated the detailed atomic positions of side-chains at position 21. The relative B-factor value of the side-chain at position 21 in the D21N mutant was higher than that of wild-type thaumatin, hinting at a greater flexibility of side-chain at 21 in the hyper-sweet D21N mutant. Furthermore, alternative conformations of Lys19, which is hydrogen-bonded to Asp21 in wild-type, were found only in the D21N mutant. Subatomic resolution analysis revealed that flexible conformations at the sites adjacent to positions 19 and 21 play a crucial role in enhancing sweet potency and may serve to enhance the complementarity of electrostatic potentials for interaction with the sweet taste receptor. | ||
| + | |||
| + | Subatomic structure of hyper-sweet thaumatin D21N mutant reveals the importance of flexible conformations for enhanced sweetness.,Masuda T, Okubo K, Murata K, Mikami B, Sugahara M, Suzuki M, Temussi PA, Tani F Biochimie. 2019 Feb;157:57-63. doi: 10.1016/j.biochi.2018.10.020. Epub 2018 Oct, 31. PMID:30389513<ref>PMID:30389513</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5x9m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Katemfe]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Masuda, T]] | [[Category: Masuda, T]] | ||
[[Category: Mikami, B]] | [[Category: Mikami, B]] | ||
Revision as of 06:55, 27 March 2019
Structure of hyper-sweet thaumatin (D21N)
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