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| - | [[Image:1mnl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mnl| PDB=1mnl | SCENE= }} | | {{STRUCTURE_1mnl| PDB=1mnl | SCENE= }} |
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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=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10029527}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10029527 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10029527}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1MNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNL OCA]. | + | 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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Sweet protein]] | | [[Category: Sweet protein]] |
| | [[Category: Sweet receptor binding]] | | [[Category: Sweet receptor binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:27:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:28:55 2008'' |
Revision as of 21:28, 2 July 2008
Template:STRUCTURE 1mnl
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
Template:ABSTRACT PUBMED 10029527
About this Structure
1MNL is a Single protein structure of sequence from Dioscoreophyllum cumminsii. Full experimental information is available from 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:10029527
Page seeded by OCA on Thu Jul 3 00:28:55 2008
