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| | ==HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES== | | ==HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES== |
| - | <StructureSection load='1mnl' size='340' side='right'caption='[[1mnl]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | + | <StructureSection load='1mnl' size='340' side='right'caption='[[1mnl]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1mnl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Diocu Diocu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MNL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1mnl]] 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=1MNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MNL 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=1mnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mnl OCA], [http://pdbe.org/1mnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mnl RCSB], [http://www.ebi.ac.uk/pdbsum/1mnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mnl ProSAT]</span></td></tr> | + | </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=1mnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mnl OCA], [https://pdbe.org/1mnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mnl RCSB], [https://www.ebi.ac.uk/pdbsum/1mnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mnl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU]] Taste-modifying protein; intensely sweet-tasting protein. | + | [https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diocu]] | + | [[Category: Dioscoreophyllum cumminsii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, H J]] | + | [[Category: Chang H-J]] |
| - | [[Category: Jo, J M]] | + | [[Category: Jo J-M]] |
| - | [[Category: Jung, J W]] | + | [[Category: Jung J-W]] |
| - | [[Category: Lee, J H]] | + | [[Category: Lee J-H]] |
| - | [[Category: Lee, S Y]] | + | [[Category: Lee S-Y]] |
| - | [[Category: Lee, W]] | + | [[Category: Lee W]] |
| - | [[Category: Alpha/beta motif]]
| + | |
| - | [[Category: Sweet protein]]
| + | |
| - | [[Category: Sweet receptor binding]]
| + | |
| Structural highlights
Function
MONA_DIOCU Taste-modifying protein; intensely sweet-tasting protein.
Publication Abstract from PubMed
Single-chain monellin (SCM), which is an engineered 94-residue polypeptide, has proven to be as sweet as native two-chain monellin. SCM is more stable than the native monellin for both heat and acidic environments. Data from gel filtration HPLC and NMR indicate that the SCM exists as a monomer in aqueous solution. The solution structure of SCM has been determined by nuclear magnetic resonance (NMR) spectroscopy and dynamical simulated annealing calculations. A stable alpha-helix spanning residues Phe11-Ile26 and an antiparallel beta-sheet formed by residues 2-5, 36-38, 41-47, 54-64, 69-75, and 83-88 have been identified. The sheet was well defined by backbone-backbone NOEs, and the corresponding beta-strands were further confirmed by hydrogen bond networks based on amide hydrogen exchange data. Strands beta2 and beta3 are connected by a small bulge comprising residues Ile38-Cys41. A total of 993 distance and 56 dihedral angle restraints were used for simulated annealing calculations. The final simulated annealing structures (<SA>k) converged well with a root-mean-square deviation (rmsd) between backbone atoms of 0.49 A for secondary structural regions and 0.70 A for backbone atoms excluding two loop regions. The average restraint energy-minimized (REM) structure exhibited root-mean-square deviations of 1.19 A for backbone atoms and 0.85 A for backbone atoms excluding two loop regions with respect to 20 <SA>k structures. The solution structure of SCM revealed that the long alpha-helix was folded into the concave side of a six-stranded antiparallel beta-sheet. The side chains of Tyr63 and Asp66 which are common to all sweet peptides showed an opposite orientation relative to H1 helix, and they were all solvent-exposed. Residues at the proposed dimeric interface in the X-ray structure were observed to be mostly solvent-exposed and demonstrated high degrees of flexibility.
Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations.,Lee SY, Lee JH, Chang HJ, Cho JM, Jung JW, Lee W Biochemistry. 1999 Feb 23;38(8):2340-6. PMID:10029527[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee SY, Lee JH, Chang HJ, Cho JM, Jung JW, Lee W. Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations. Biochemistry. 1999 Feb 23;38(8):2340-6. PMID:10029527 doi:http://dx.doi.org/10.1021/bi9822731
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