7QCC
Williams-Beuren syndrome related methyltransferase WBSCR27 in apo-form
Summary for 7QCC
| Entry DOI | 10.2210/pdb7qcc/pdb |
| NMR Information | BMRB: 27578 |
| Descriptor | Methyltransferase-like 27 (1 entity in total) |
| Functional Keywords | williams-beuren syndrome, sam-dependent methyltransferase, rossman fold, class i methyltransferases, transferase |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 25988.48 |
| Authors | Polshakov, V.I.,Mariasina, S.S.,Chang, C.-F. (deposition date: 2021-11-23, release date: 2021-12-29, Last modification date: 2024-06-19) |
| Primary citation | 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 Cited by 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: 35782865DOI: 10.3389/fmolb.2022.865743 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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