@article{1c1bc80d643b46c8b07e80b9983b1c0c,
title = "NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome",
abstract = "Williams-Beuren syndrome is a genetic disorder characterized by physiological and mental abnormalities, and is caused by hemizygous deletion of several genes in chromosome 7. One of the removed genes encodes the WBSCR27 protein. Bioinformatic analysis of the sequence of WBSCR27 indicates that it belongs to the family of SAM-dependent methyltransferases. However, exact cellular functions of this protein or phenotypic consequences of its deficiency are still unknown. Here we report nearly complete 1H, 15N, and 13C chemical shifts assignments of the 26 kDa WBSCR27 protein from Mus musculus in complex with the cofactor S-adenosyl-l-methionine (SAM). Analysis of the assigned chemical shifts allowed us to characterize the protein{\textquoteright}s secondary structure and backbone dynamics. The topology of the protein{\textquoteright}s fold confirms the assumption that the WBSCR27 protein belongs to the family of class I methyltransferases.",
keywords = "Protein NMR, Resonance assignment, SAM-dependent methyltransferases, Secondary structure, Williams-Beuren syndrome",
author = "Mariasina, {Sofia S.} and Petrova, {Olga A.} and Osterman, {Ilya A.} and Sergeeva, {Olga V.} and Efimov, {Sergey V.} and Klochkov, {Vladimir V.} and Sergiev, {Petr V.} and Dontsova, {Olga A.} and Huang, {Tai huang} and Chang, {Chi Fon} and Polshakov, {Vladimir I.}",
note = "Funding Information: Fig. 3 Amino acid sequence, protein chain mobility and secondary structure of the Mus musculus WBSCR27. Values of order parameters (S2) predicted by TALOS + are shown in open circles. Values of experimentally measured 15N{1H}NOEs are shown as black circles. Results of the secondary structure prediction by TALOS+ (Shen et al. 2009) are shown as vertical bars (positive for β-strands and negative Fig. 4 a Packing of class I SAM-dependent methyltransferases, which have the α/β/α sandwich topology with the central core formed by seven β-strands (Fauman et al. 1999). b Topology of WBSCR27 protein in complex with SAM for α-helices). Absolute values of bars are equal to the probability of existence of corresponding amino acid residue in one or another element of the secondary structure. The drawings show the predicted secondary structure of the WBSCR27 based on NMR chemical shift assignments Acknowledgements The Russian Foundation for Basic Research (Grant 17-04-00852) supported the NMR studies. WBSCR27 expression and purification work was supported by Russian Science Foundation Grant 17-75-30027. The authors are grateful to Daniela Rhodes (MRS LMB, Cambridge, UK) for providing pET30aTEV vector. The 850 MHz NMR experiments were carried out using the equipment of the High-Field Nuclear Magnetic Resonance Center (HFNMRC) supported by Academia Sinica, Taipei, Taiwan. Funding Information: The Russian Foundation for Basic Research (Grant 17-04-00852) supported the NMR studies. WBSCR27 expression and purification work was supported by Russian Science Foundation Grant 17-75-30027. The authors are grateful to Daniela Rhodes (MRS LMB, Cambridge, UK) for providing pET30aTEV vector. The 850?MHz NMR experiments were carried out using the equipment of the High-Field Nuclear Magnetic Resonance Center (HFNMRC) supported by Academia Sinica, Taipei, Taiwan. Publisher Copyright: {\textcopyright} 2018, Springer Science+Business Media B.V., part of Springer Nature.",
year = "2018",
month = oct,
day = "1",
doi = "10.1007/s12104-018-9827-2",
language = "English",
volume = "12",
pages = "303--308",
journal = "Biomolecular NMR Assignments",
issn = "1874-2718",
publisher = "Springer Netherlands",
number = "2",
}