7QCC

Williams-Beuren syndrome related methyltransferase WBSCR27 in apo-form

7QCC の概要

• エントリーDOI: 10.2210/pdb7qcc/pdb
• NMR情報: BMRB: 27578
• 分子名称: Methyltransferase-like 27 (1 entity in total)
• 機能のキーワード: williams-beuren syndrome, sam-dependent methyltransferase, rossman fold, class i methyltransferases, transferase
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25988.48

構造登録者

Polshakov, V.I.,Mariasina, S.S.,Chang, C.-F. (登録日: 2021-11-23, 公開日: 2021-12-29, 最終更新日: 2024-06-19)

主引用文献

Mariasina, S.S.,Chang, C.F.,Navalayeu, T.L.,Chugunova, A.A.,Efimov, S.V.,Zgoda, V.G.,Ivlev, V.A.,Dontsova, O.A.,Sergiev, P.V.,Polshakov, V.I.
Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function.
Front Mol Biosci, 9:865743-865743, 2022

PubMed Abstract: Williams-Beuren syndrome (WBS) is a genetic disorder associated with the hemizygous deletion of several genes in chromosome 7, encoding 26 proteins. Malfunction of these proteins induce multisystemic failure in an organism. While biological functions of most proteins are more or less established, the one of methyltransferase WBSCR27 remains elusive. To find the substrate of methylation catalyzed by WBSCR27 we constructed mouse cell lines with a gene knockout and studied the obtained cells using several molecular biology and mass spectrometry techniques. We attempted to pinpoint the methylation target among the RNAs and proteins, but in all cases neither a direct substrate has been identified nor the protein partners have been detected. To reveal the nature of the putative methylation substrate we determined the solution structure and studied the conformational dynamic properties of WBSCR27 in apo state and in complex with S-adenosyl-L-homocysteine (SAH). The protein core was found to form a canonical Rossman fold common for Class I methyltransferases. N-terminus of the protein and the β6-β7 loop were disordered in apo-form, but binding of SAH induced the transition of these fragments to a well-formed substrate binding site. Analyzing the structure of this binding site allows us to suggest potential substrates of WBSCR27 methylation to be probed in further research.

PubMed: 35782865
DOI: 10.3389/fmolb.2022.865743

実験手法

SOLUTION NMR