View source for 1fuw


==SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A DOUBLE MUTANT SINGLE-CHAIN MONELLIN(SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY==
<StructureSection load='1fuw' size='340' side='right'caption='[[1fuw]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fuw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuw OCA], [https://pdbe.org/1fuw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuw RCSB], [https://www.ebi.ac.uk/pdbsum/1fuw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MONB_DIOCU MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.
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== Publication Abstract from PubMed ==
Single-chain monellin (SCM), which is an engineered 94-residue polypeptide, has been characterized as being as sweet as native two-chain monellin. Data from gel-filtration high performance liquid chromatography and NMR has proven that SCM exists as a monomer in aqueous solution. In order to determine the structural origin of the taste of sweetness, we engineered several mutant SCM proteins by mutating Glu(2), Asp(7), and Arg(39) residues, which are responsible for sweetness. In this study, we present the solution structure, backbone dynamics, and stability of mutant SCM proteins using circular dichroism, fluorescence, and NMR spectroscopy. Based on the NMR data, a stable alpha-helix and five-stranded antiparallel beta-sheet were identified for double mutant SCM. Strands beta1 and beta2 are connected by a small bulge, and the disruption of the first beta-strand were observed with SCM(DR) comprising residues of Ile(38)-Cys(41). The dynamical and folding characteristics from circular dichroism, fluorescence, and backbone dynamics studies revealed that both wild type and mutant proteins showed distinct dynamical as well as stability differences, suggesting the important role of mutated residues in the sweet taste of SCM. Our results will provide an insight into the structural origin of sweet taste as well as the mutational effect in the stability of the engineered sweet protein SCM.

Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. structural origin of sweetness.,Sung YH, Shin J, Chang HJ, Cho JM, Lee W J Biol Chem. 2001 Jun 1;276(22):19624-30. Epub 2001 Mar 7. PMID:11279156<ref>PMID:11279156</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1fuw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Dioscoreophyllum cumminsii]]
[[Category: Large Structures]]
[[Category: Jung J]]
[[Category: Lee W]]
[[Category: Shin J]]
[[Category: Sung YH]]