Petr Sergiev and Olga Dontsova have co-authored a paper “Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function” that has been recently published in Frontiers in Molecular Biosciences journal. The study is focused on Williams-Beuren syndrome (WBS), a genetic disorder associated with the hemizygous deletion of several genes in chromosome 7, encoding 26 proteins. Loss of these proteins induces multisystemic failure in an organism. While biological functions of most proteins are more or less established, the one of methyltransferase WBSCR27 remains elusive. To reveal the nature of the putative methylation substrate the researchers determined the solution structure and studied the conformational dynamic properties of WBSCR27 in free state and in complex with S-adenosyl-L-homocysteine. They have found that N-terminus of the protein and the β6–β7 loop were disordered in apo-form, but binding of S-adenosyl-L-homocysteine induced the transition of these fragments to a well-formed substrate binding site. The researchers suggest that analyzing the structure of this binding site allows us to suggest potential substrates of WBSCR27 methylation to be probed in further research. Full text of the paper is available here.