{"_buckets": {"deposit": "f6fd17b5-43f4-4392-9346-f1de42d36c43"}, "_deposit": {"id": "5108", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "5108"}, "status": "published"}, "_oai": {"id": "oai:nagoya.repo.nii.ac.jp:00005108"}, "item_10_biblio_info_6": {"attribute_name": "\u66f8\u8a8c\u60c5\u5831", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2005-07", "bibliographicIssueDateType": "Issued"}, "bibliographicIssueNumber": "3", "bibliographicPageEnd": "403", "bibliographicPageStart": "393", "bibliographicVolumeNumber": "1708", "bibliographic_titles": [{"bibliographic_title": "Biochimica et Biophysica Acta"}]}]}, "item_10_description_4": {"attribute_name": "\u6284\u9332", "attribute_value_mlt": [{"subitem_description": "The H+-pyrophosphatase (H+-PPase) consists of a single polypeptide, containing 16\nor 17 transmembrane domains. To determine the higher order oligomeric state of\nStreptomyces coelicolor H+-PPase, we constructed a series of cysteine substitution\nmutants and expressed them in Escherichia coli. Firstly, we analyzed the formation of\ndisulfide bonds, promoted by copper, in mutants with single cysteine substitutions. 28 of\n39 mutants formed disulfide bonds, including S545C, a substitution at the periplasmic\nside. The formation of intermolecular disulfide bonds suppressed the enzyme activity of\nseveral, where the substituted residues were located in the cytosol. Creating disulfide\nlinks in the cytosol may interfere with the enzyme\u2019s catalytic function. Secondly, we\nprepared double mutants by introducing second cysteine substitutions into the S545C\nmutant. These double-cysteine mutants produced cross-linked complexes, estimated to\nbe at least tetramers and possibly hexamers. Thirdly, we co-expressed epitope-tagged,\nwild type and inactive mutant H+-PPases in E. coli and confirmed the formation of\noligomers by co-purifying one subunit using the epitope tag used to label the other. The\nenzyme activity of these oligomers was markedly suppressed. We propose that H+-PPase\nis present as an oligomer made up of at least two or three sets of dimers.", "subitem_description_type": "Abstract"}]}, "item_10_identifier_60": {"attribute_name": "URI", "attribute_value_mlt": [{"subitem_identifier_type": "HDL", "subitem_identifier_uri": "http://hdl.handle.net/2237/6661"}]}, "item_10_publisher_32": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": "Elsevier"}]}, "item_10_select_15": {"attribute_name": "\u8457\u8005\u7248\u30d5\u30e9\u30b0", "attribute_value_mlt": [{"subitem_select_item": "publisher"}]}, "item_10_text_14": {"attribute_name": "\u30d5\u30a9\u30fc\u30de\u30c3\u30c8", "attribute_value_mlt": [{"subitem_text_value": "application/pdf"}]}, "item_creator": {"attribute_name": "\u8457\u8005", "attribute_type": "creator", "attribute_value_mlt": [{"creatorNames": [{"creatorName": "Mimura, Hisatoshi"}], "nameIdentifiers": [{"nameIdentifier": "12640", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Nakanishi, Yoichi"}], "nameIdentifiers": [{"nameIdentifier": "12641", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "Maeshima, Masayoshi"}], "nameIdentifiers": [{"nameIdentifier": "12642", "nameIdentifierScheme": "WEKO"}]}, {"creatorNames": [{"creatorName": "\u524d\u5cf6, \u6b63\u7fa9"}], "nameIdentifiers": [{"nameIdentifier": "12643", "nameIdentifierScheme": "WEKO"}]}]}, "item_files": {"attribute_name": "\u30d5\u30a1\u30a4\u30eb\u60c5\u5831", "attribute_type": "file", "attribute_value_mlt": [{"accessrole": "open_date", "date": [{"dateType": "Available", "dateValue": "2018-02-19"}], "displaytype": "detail", "download_preview_message": "", "file_order": 0, "filename": "2005-BBA-ScPP.pdf", "filesize": [{"value": "918.3 kB"}], "format": "application/pdf", "future_date_message": "", "is_thumbnail": false, "licensetype": "license_free", "mimetype": "application/pdf", "size": 918300.0, "url": {"label": "2005-BBA-ScPP.pdf", "url": "https://nagoya.repo.nii.ac.jp/record/5108/files/2005-BBA-ScPP.pdf"}, "version_id": "65a18e8b-6e03-4ae6-9895-3d06eff16d58"}]}, "item_keyword": {"attribute_name": "\u30ad\u30fc\u30ef\u30fc\u30c9", "attribute_value_mlt": [{"subitem_subject": "Disulfide bond", "subitem_subject_scheme": "Other"}, {"subitem_subject": "H+-pyrophosphatase", "subitem_subject_scheme": "Other"}, {"subitem_subject": "Oligomerization", "subitem_subject_scheme": "Other"}, {"subitem_subject": "Proton pump", "subitem_subject_scheme": "Other"}]}, "item_language": {"attribute_name": "\u8a00\u8a9e", "attribute_value_mlt": [{"subitem_language": "eng"}]}, "item_resource_type": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"resourcetype": "journal article", "resourceuri": "http://purl.org/coar/resource_type/c_6501"}]}, "item_title": "Oligomerization of H+-pyrophosphatase and its structural and functional consequences", "item_titles": {"attribute_name": "\u30bf\u30a4\u30c8\u30eb", "attribute_value_mlt": [{"subitem_title": "Oligomerization of H+-pyrophosphatase and its structural and functional consequences"}]}, "item_type_id": "10", "owner": "1", "path": ["643/666/667"], "permalink_uri": "http://hdl.handle.net/2237/6661", "pubdate": {"attribute_name": "\u516c\u958b\u65e5", "attribute_value": "2006-06-30"}, "publish_date": "2006-06-30", "publish_status": "0", "recid": "5108", "relation": {}, "relation_version_is_last": true, "title": ["Oligomerization of H+-pyrophosphatase and its structural and functional consequences"], "weko_shared_id": null}