{"created":"2023-06-26T11:00:33.110251+00:00","id":1050,"links":{},"metadata":{"_buckets":{"deposit":"c252d964-ea9f-465d-bd47-d114ba8005f0"},"_deposit":{"created_by":26,"id":"1050","owners":[26],"pid":{"revision_id":0,"type":"depid","value":"1050"},"status":"published"},"_oai":{"id":"oai:oist.repo.nii.ac.jp:00001050","sets":["6:74"]},"author_link":["5789","5792","5790","5791"],"item_10001_biblio_info_7":{"attribute_name":"Bibliographic Information","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2018-11-08","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"3","bibliographicPageEnd":"170","bibliographicPageStart":"166","bibliographicVolumeNumber":"58","bibliographic_titles":[{},{"bibliographic_title":"Biochemistry","bibliographic_titleLang":"en"}]}]},"item_10001_creator_3":{"attribute_name":"Author","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Chouhan, Bhanu Pratap Singh"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Maimaiti, Shayida"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Gade, Madhuri"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Laurino, Paola"}],"nameIdentifiers":[{}]}]},"item_10001_description_5":{"attribute_name":"Abstract","attribute_value_mlt":[{"subitem_description":"Methyltransferases (MTases) are superfamilies of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (SAM), a nucleoside-based cofactor, to a wide variety of substrates such as DNA, RNA, proteins, small molecules, and lipids. Depending upon their structural features, the MTases can be further classified into different classes; we consider exclusively the largest class of MTases, the Rossmann-fold MTases. It has been shown that the nucleoside cofactor-binding Rossmann enzymes, particularly the nicotinamide adenine dinucleotide (NAD)-, flavin adenine dinucleotide (FAD)-, and SAM-binding MTases enzymes, share common binding motifs that include a Gly-rich loop region that interacts with the cofactor and a highly conserved acidic residue (Asp/Glu) that interacts with the ribose moiety of the cofactor. Here, we observe that the Gly-rich loop region of the Rossmann MTases adapts a specific type II′ β-turn in the proximity of the cofactor (<4 Å), and it appears to be a key feature of these superfamilies. Additionally, we demonstrate that the conservation of this β-turn could play a critical role in the enzyme–cofactor interaction, thereby shedding new light on the structural conformation of the Gly-rich loop region from Rossmann MTases.","subitem_description_type":"Other"}]},"item_10001_publisher_8":{"attribute_name":"Publisher","attribute_value_mlt":[{"subitem_publisher":"American Chemical Society"}]},"item_10001_relation_13":{"attribute_name":"PubMedNo.","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"info:pmid/30406995","subitem_relation_type_select":"PMID"}}]},"item_10001_relation_14":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"info:doi/10.1021/acs.biochem.8b00994","subitem_relation_type_select":"DOI"}}]},"item_10001_relation_17":{"attribute_name":"Related site","attribute_value_mlt":[{"subitem_relation_type_id":{"subitem_relation_type_id_text":"https://pubs.acs.org/doi/10.1021/acs.biochem.8b00994","subitem_relation_type_select":"URI"}}]},"item_10001_rights_15":{"attribute_name":"Rights","attribute_value_mlt":[{"subitem_rights":"© 2018 American Chemical Society"},{"subitem_rights":"This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.biochem.8b00994."}]},"item_10001_source_id_9":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"0006-2960","subitem_source_identifier_type":"ISSN"},{"subitem_source_identifier":"1520-4995","subitem_source_identifier_type":"ISSN"}]},"item_10001_version_type_20":{"attribute_name":"Author's flag","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-11-08"}],"displaytype":"detail","filename":"ACS_Biochemistry_Manuscript.pdf","filesize":[{"value":"801.3 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"ACS_Biochemistry_Manuscript","url":"https://oist.repo.nii.ac.jp/record/1050/files/ACS_Biochemistry_Manuscript.pdf"},"version_id":"703fe09a-5ba2-4e2e-8611-b4b101b7ac18"},{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2019-11-08"}],"displaytype":"detail","filename":"ACS_Biochemistry_Manuscript_Supplementary.pdf","filesize":[{"value":"3.5 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"ACS_Biochemistry_Manuscript_Supplementary","url":"https://oist.repo.nii.ac.jp/record/1050/files/ACS_Biochemistry_Manuscript_Supplementary.pdf"},"version_id":"8be041d0-055b-4256-a7c3-962abf0f1081"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"Rossmann-Fold Methyltransferases: Taking a “β-Turn” around Their Cofactor, S-Adenosylmethionine","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"Rossmann-Fold Methyltransferases: Taking a “β-Turn” around Their Cofactor, S-Adenosylmethionine","subitem_title_language":"en"}]},"item_type_id":"10001","owner":"26","path":["74"],"pubdate":{"attribute_name":"公開日","attribute_value":"2019-08-05"},"publish_date":"2019-08-05","publish_status":"0","recid":"1050","relation_version_is_last":true,"title":["Rossmann-Fold Methyltransferases: Taking a “β-Turn” around Their Cofactor, S-Adenosylmethionine"],"weko_creator_id":"26","weko_shared_id":26},"updated":"2023-06-26T11:57:34.230378+00:00"}