{"@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/1362825893668815744.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1126/science.1259680"}},{"identifier":{"@type":"URI","@value":"https://www.science.org/doi/pdf/10.1126/science.1259680"}}],"dc:title":[{"@value":"A designed supramolecular protein assembly with in vivo enzymatic activity"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n                    The generation of new enzymatic activities has mainly relied on repurposing the interiors of preexisting protein folds because of the challenge in designing functional, three-dimensional protein structures from first principles. Here we report an artificial metallo-β-lactamase, constructed via the self-assembly of a structurally and functionally unrelated, monomeric redox protein into a tetrameric assembly that possesses catalytic zinc sites in its interfaces. The designed metallo-β-lactamase is functional in the\n                    <jats:italic>Escherichia coli</jats:italic>\n                    periplasm and enables the bacteria to survive treatment with ampicillin. In vivo screening of libraries has yielded a variant that displays a catalytic proficiency [(\n                    <jats:italic>k</jats:italic>\n                    <jats:sub>cat</jats:sub>\n                    /\n                    <jats:italic>K</jats:italic>\n                    <jats:sub>m</jats:sub>\n                    )/\n                    <jats:italic>k</jats:italic>\n                    <jats:sub>uncat</jats:sub>\n                    ] for ampicillin hydrolysis of 2.3 × 10\n                    <jats:sup>6</jats:sup>\n                    and features the emergence of a highly mobile loop near the active site, a key component of natural β-lactamases to enable substrate interactions.\n                  </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1382825893668815745","@type":"Researcher","foaf:name":[{"@value":"Woon Ju Song"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0356, USA."}]},{"@id":"https://cir.nii.ac.jp/crid/1382825893668815744","@type":"Researcher","foaf:name":[{"@value":"F. Akif Tezcan"}],"jpcoar:affiliationName":[{"@value":"Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0356, USA."}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00368075"},{"@type":"EISSN","@value":"10959203"}],"prism:publicationName":[{"@value":"Science"}],"dc:publisher":[{"@value":"American Association for the Advancement of Science (AAAS)"}],"prism:publicationDate":"2014-12-19","prism:volume":"346","prism:number":"6216","prism:startingPage":"1525","prism:endingPage":"1528"},"reviewed":"false","url":[{"@id":"https://www.science.org/doi/pdf/10.1126/science.1259680"}],"createdAt":"2014-12-19","modifiedAt":"2024-01-10","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050295834375976832","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Rational Design of Domain‐Swapping‐Based c‐Type Cytochrome Heterodimers by Using Chimeric Proteins"},{"@value":"Rational Design of Domain‐Swapping‐Based <i>c</i>‐Type Cytochrome Heterodimers by Using Chimeric Proteins"},{"@value":"Rational design of domain-swapping-based c-type cytochrome heterodimers by using chimeric proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1050577309352733312","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Domain-swapped cytochrome cb562 dimer and its nanocage encapsulating a Zn-SO4 cluster in the internal cavity"},{"@value":"Domain-swapped cytochrome cb<sub>562</sub>dimer and its nanocage encapsulating a Zn–SO<sub>4</sub>cluster in the internal cavity"}]},{"@id":"https://cir.nii.ac.jp/crid/1050863782914881792","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Artificial metalloenzymes based on protein assembly"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002216616397184","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Crystal Engineering of Self-Assembled Porous Protein Materials in Living Cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004233216499072","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A Well-Defined Osmium–Cupin Complex: Hyperstable Artificial Osmium Peroxygenase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004237005093120","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Arginine Residues Provide a Multivalent Effect for Cellular Uptake of a Hemoprotein Assembly"}]},{"@id":"https://cir.nii.ac.jp/crid/1360009142871985280","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Directed Evolution of a Cp*Rh<sup>III</sup>‐Linked Biohybrid Catalyst Based on a Screening Platform with Affinity Purification"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283690855251072","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Design and construction of self-assembling supramolecular protein complexes using artificial and fusion proteins as nanoscale building blocks"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283691128476800","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Engineering of protein assemblies within cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092434100096","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Enzyme-Directed Functionalization of 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addition"}]},{"@id":"https://cir.nii.ac.jp/crid/1360869856022835584","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A thiopyridine-bound mirror-image copper center in an artificial non-heme metalloenzyme"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975843220206976","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Biocompatibility and therapeutic potential of glycosylated albumin artificial metalloenzymes"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975846030525952","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Supramolecular dimerization of a hexameric hemoprotein <i>via</i> multiple pyrene-pyrene interactions"}]},{"@id":"https://cir.nii.ac.jp/crid/1390002184880674176","@type":"Article","resourceType":"学術雑誌論文(journal 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