1mnl: Difference between revisions

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{{Seed}}
[[Image:1mnl.png|left|200px]]


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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==
The line below this paragraph, containing "STRUCTURE_1mnl", creates the "Structure Box" on the page.
<StructureSection load='1mnl' size='340' side='right'caption='[[1mnl]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_1mnl|  PDB=1mnl  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.
<div style="background-color:#fffaf0;">
== 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 (&lt;SA&gt;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 &lt;SA&gt;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.


===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===
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<ref>PMID:10029527</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_10029527}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1mnl" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 10029527 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_10029527}}
__TOC__
 
</StructureSection>
==About this Structure==
1MNL is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10029527 10029527]
[[Category: Dioscoreophyllum cumminsii]]
[[Category: Dioscoreophyllum cumminsii]]
[[Category: Single protein]]
[[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]]
 
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Retrieved from "https://proteopedia.org/1mnl"