1fuw
From Proteopedia
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SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A DOUBLE MUTANT SINGLE-CHAIN MONELLIN(SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Overview
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.
About this Structure
1FUW is a Single protein structure of sequence from Dioscoreophyllum cumminsii. Full crystallographic information is available from OCA.
Reference
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
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