Structural and functional analysis of miraculin-like protein from Vitis vinifera

Publication date: Available online 27 August 2018Source: Biochimica et Biophysica Acta (BBA) - Proteins and ProteomicsAuthor(s): So-ichiro Ohkura, Misaho Hori, Kazuki Saitoh, Takumi Okuzawa, Ikuko Okamoto, Nayuta Furukawa, Akiko Shimizu-IbukaAbstractThe so-called miraculin-like proteins (MLPs) are homologous to miraculin, a homodimeric protein with taste-modifying activity that converts sourness into sweetness. The identity between MLPs and miraculin generally ranges from 30% to 55%, and both MLPs and miraculin are categorized into the Kunitz-type soybean trypsin inhibitor (STI) family. MLP from grape (Vitis vinifera; vvMLP) exhibits significant homology to miraculin (61% identity), suggesting that vvMLP possesses miraculin-like properties. The results of size-exclusion chromatography and sensory analysis illustrated that vvMLP exists as a monomer in solution with no detectable taste-modifying activity. Crystal structure determination revealed that vvMLP exists as a β-trefoil fold, similarly as other MLPs and Kunitz-type protein inhibitors. The conformation of the loops, including the so-called reactive loop in the STI family, was substantially different between vvMLP and STI. Recombinant vvMLP had inhibitory activity against trypsin (Ki = 13.7 μM), indicating that the protein can act as a moderate trypsin inhibitor.

Source: Biochimica et Biophysica Acta (BBA) Proteins and Proteomics - August 28, 2018 Category: Biochemistry Source Type: research