4PON
The crystal structure of a putative SAM-dependent methyltransferase, YtqB, from Bacillus subtilis
Summary for 4PON
| Entry DOI | 10.2210/pdb4pon/pdb |
| Related | 4POO |
| Descriptor | Putative RNA methylase (2 entities in total) |
| Functional Keywords | rossmann-like fold, a putative methyltransferase, s-adenosyl-l-methionine, transferase |
| Biological source | Bacillus subtilis subsp. spizizenii |
| Total number of polymer chains | 2 |
| Total formula weight | 43579.66 |
| Authors | Park, S.C.,Song, W.S.,Yoon, S.I. (deposition date: 2014-02-26, release date: 2014-04-02, Last modification date: 2023-11-08) |
| Primary citation | Park, S.C.,Song, W.S.,Yoon, S.I. Structural analysis of a putative SAM-dependent methyltransferase, YtqB, from Bacillus subtilis Biochem.Biophys.Res.Commun., 446:921-926, 2014 Cited by PubMed Abstract: S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTases) methylate diverse biological molecules using a SAM cofactor. The ytqB gene of Bacillus subtilis encodes a putative MTase and its biological function has never been characterized. To reveal the structural features and the cofactor binding mode of YtqB, we have determined the crystal structures of YtqB alone and in complex with its cofactor, SAM, at 1.9 Å and 2.2 Å resolutions, respectively. YtqB folds into a β-sheet sandwiched by two α-helical layers, and assembles into a dimeric form. Each YtqB monomer contains one SAM binding site, which shapes SAM into a slightly curved conformation and exposes the reactive methyl group of SAM potentially to a substrate. Our comparative structural analysis of YtqB and its homologues indicates that YtqB is a SAM-dependent class I MTase, and provides insights into the substrate binding site of YtqB. PubMed: 24637210DOI: 10.1016/j.bbrc.2014.03.026 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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