{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670319778726272.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1074/jbc.m109090200"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925820877382?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925820877382?httpAccept=text/plain"}},{"identifier":{"@type":"URI","@value":"https://syndication.highwire.org/content/doi/10.1074/jbc.M109090200"}},{"identifier":{"@type":"PMID","@value":"11704672"}},{"identifier":{"@type":"NAID","@value":"80012897597"}}],"dc:title":[{"@value":"Crystal Structure of Quinohemoprotein Amine Dehydrogenase from Pseudomonas putida"}],"description":[{"notation":[{"@value":"The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383670319778726276","@type":"Researcher","foaf:name":[{"@value":"Atsuko Satoh"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726281","@type":"Researcher","foaf:name":[{"@value":"Jong-Keun Kim"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726273","@type":"Researcher","foaf:name":[{"@value":"Ikuko Miyahara"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726145","@type":"Researcher","foaf:name":[{"@value":"Bart Devreese"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726146","@type":"Researcher","foaf:name":[{"@value":"Isabel Vandenberghe"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726278","@type":"Researcher","foaf:name":[{"@value":"Ayse Hacisalihoglu"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726272","@type":"Researcher","foaf:name":[{"@value":"Toshihide Okajima"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726144","@type":"Researcher","foaf:name":[{"@value":"Shun'ichi Kuroda"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726280","@type":"Researcher","foaf:name":[{"@value":"Osao Adachi"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726279","@type":"Researcher","foaf:name":[{"@value":"Johannis A. Duine"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726274","@type":"Researcher","foaf:name":[{"@value":"Jozef Van Beeumen"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726275","@type":"Researcher","foaf:name":[{"@value":"Katsuyuki Tanizawa"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670319778726277","@type":"Researcher","foaf:name":[{"@value":"Ken Hirotsu"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219258"}],"prism:publicationName":[{"@value":"Journal of Biological Chemistry"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"2002-01","prism:volume":"277","prism:number":"4","prism:startingPage":"2830","prism:endingPage":"2834"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/","http://creativecommons.org/licenses/by/4.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S0021925820877382?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S0021925820877382?httpAccept=text/plain"},{"@id":"https://syndication.highwire.org/content/doi/10.1074/jbc.M109090200"}],"createdAt":"2002-07-26","modifiedAt":"2022-01-05","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Models,%20Molecular","dc:title":"Models, Molecular"},{"@id":"https://cir.nii.ac.jp/all?q=Aspartic%20Acid","dc:title":"Aspartic Acid"},{"@id":"https://cir.nii.ac.jp/all?q=Oxidoreductases%20Acting%20on%20CH-NH%20Group%20Donors","dc:title":"Oxidoreductases Acting on CH-NH Group 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