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5z1p
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==Structural basis of the improved sweetness and stability of the single-chain sweet-tasting protein monellin (MNEI)== | ==Structural basis of the improved sweetness and stability of the single-chain sweet-tasting protein monellin (MNEI)== | ||
| - | <StructureSection load='5z1p' size='340' side='right' caption='[[5z1p]], [[Resolution|resolution]] 1.89Å' scene=''> | + | <StructureSection load='5z1p' size='340' side='right'caption='[[5z1p]], [[Resolution|resolution]] 1.89Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5z1p]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z1P OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5z1p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z1P FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89Å</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=5z1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z1p OCA], [https://pdbe.org/5z1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z1p RCSB], [https://www.ebi.ac.uk/pdbsum/5z1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z1p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.[https://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein. |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The sweet protein monellin has an intensely sweet potency but limited stability. We have identified a double-sites mutant (E2N/E23A) of the single-chain monellin (MNEI) with both improved sweetness (about 3-fold) and thermostability (10 degrees C). However, the structural basis of its superior properties remains elusive until now. Herein we report its crystal structure at a resolution 1.90A. Similar to the wild-type, E2N/E23A adopts a wedge-shaped structure consisting of a five-strand beta-sheet partially "wrapped" around an alpha-helix. However, distinguishing parts were present in the loops region, including a remarkable conformation shift from beta-strand to loop around residue R39. Molecular docking revealed the persistence of conserved protein-receptor interface and formation of new intermolecular ionic bonds in the E2N/E23A-receptor complex involving the taste-active residue R39 of the sweet protein, which could account for its significant improvement of sweetness. On the other hand, a rearrangement of intramolecular interaction network including the C-H ... pi bond between A23 and F89 that led to enhanced hydrophobicity in the protein core, could be correlated with its improved thermostability. Furthermore, two new sweeter mutants of MNEI were created. These findings highlight the critical roles of key sweetness determinant residue R39 and hydrophobicity at the protein core for the sweetness and thermostability of the protein, respectively, which thus provide a deeper insight for understanding the structure-function relationship of the sweet protein as well as guidance for rational design of this unique biomacromolecule. | ||
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| + | Structure basis of the improved sweetness and thermostability of a unique double-sites single-chain sweet-tasting protein monellin (MNEI) mutant.,Zhao M, Xu X, Liu B Biochimie. 2018 Nov;154:156-163. doi: 10.1016/j.biochi.2018.08.010. Epub 2018 Sep, 6. PMID:30195051<ref>PMID:30195051</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5z1p" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Dioscoreophyllum cumminsii]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Liu B]] |
Current revision
Structural basis of the improved sweetness and stability of the single-chain sweet-tasting protein monellin (MNEI)
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