5lc7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a single chain monellin mutant: E23Q/Q28K/C41S/Y65R-MNEI== | |
| + | <StructureSection load='5lc7' size='340' side='right' caption='[[5lc7]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lc7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LC7 FirstGlance]. <br> | ||
| + | </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=5lc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lc7 OCA], [http://pdbe.org/5lc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lc7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lc7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU]] Taste-modifying protein; intensely sweet-tasting protein. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sweet proteins are a family of proteins with no structure or sequence homology, able to elicit a sweet sensation in humans through their interaction with the dimeric T1R2-T1R3 sweet receptor. In particular, monellin and its single chain derivative (MNEI) are among the sweetest proteins known to men. Starting from a careful analysis of the surface electrostatic potentials, we have designed new mutants of MNEI with enhanced sweetness. Then, we have included in the most promising variant the stabilising mutation E23Q, obtaining a construct with enhanced performances, which combines extreme sweetness to high, pH-independent, thermal stability. The resulting mutant, with a sweetness threshold of only 0.28 mg/L (25 nM) is the strongest sweetener known to date. All the new proteins have been produced and purified and the structures of the most powerful mutants have been solved by X-ray crystallography. Docking studies have then confirmed the rationale of their interaction with the human sweet receptor, hinting at a previously unpredicted role of plasticity in said interaction. | ||
| - | + | Sweeter and stronger: enhancing sweetness and stability of the single chain monellin MNEI through molecular design.,Leone S, Pica A, Merlino A, Sannino F, Temussi PA, Picone D Sci Rep. 2016 Sep 23;6:34045. doi: 10.1038/srep34045. PMID:27658853<ref>PMID:27658853</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5lc7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Merlino, A]] | [[Category: Merlino, A]] | ||
[[Category: Pica, A]] | [[Category: Pica, A]] | ||
| + | [[Category: Plant protein]] | ||
| + | [[Category: Sweet protein]] | ||
Revision as of 21:36, 5 October 2016
Crystal structure of a single chain monellin mutant: E23Q/Q28K/C41S/Y65R-MNEI
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