{"@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/1050295834376182144.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"HDL","@value":"http://hdl.handle.net/10061/8821"}},{"identifier":{"@type":"URI","@value":"https://naist.repo.nii.ac.jp/records/9107"}},{"identifier":{"@type":"DOI","@value":"10.1073/pnas.1300558110"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.1300558110"}},{"identifier":{"@type":"PMID","@value":"23818613"}},{"identifier":{"@type":"HANDLE","@value":"10061/8821"}},{"identifier":{"@type":"NAID","@value":"120005716836"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@language":"en","@value":"Structural and functional analysis of the yeast N-acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism"},{"@value":"Structural and functional analysis of the yeast\n            <i>N</i>\n            -acetyltransferase Mpr1 involved in oxidative stress tolerance via proline metabolism"}],"dc:language":"en","description":[{"type":"Abstract","notation":[{"@language":"en","@value":"Mpr1 (sigma1278b gene for proline-analog resistance 1), which was originally isolated as N-acetyltransferase detoxifying the proline analog L-azetidine-2-carboxylate, protects yeast cells from various oxidative stresses. Mpr1 mediates the L-proline and L-arginine metabolism by acetylating L-Δ1-pyrroline-5-carboxylate, leading to the L-arginine-dependent production of nitric oxide, which confers oxidative stress tolerance. Mpr1 belongs to the Gcn5-related N-acetyltransferase (GNAT) superfamily, but exhibits poor sequence homology with the GNAT enzymes and unique substrate specificity. Here, we present the X-ray crystal structure of Mpr1 and its complex with the substrate cis-4-hydroxy-L-proline at 1.9 and 2.3 A resolution, respectively. Mpr1 is folded into α/β-structure with eight-stranded mixed β-sheets and six α-helices. The substrate binds to Asn135 and the backbone amide of Asn172 and Leu173, and the predicted acetyl-CoA-binding site is located near the backbone amide of Phe138 and the side chain of Asn178. Alanine substitution of Asn178, which can interact with the sulfur of acetyl-CoA, caused a large reduction in the apparent kcat value. The replacement of Asn135 led to a remarkable increase in the apparent Km value. These results indicate that Asn178 and Asn135 play an important role in catalysis and substrate recognition, respectively. Such a catalytic mechanism has not been reported in the GNAT proteins. Importantly, the amino acid substitutions in these residues increased the L-Δ1-pyrroline-5-carboxylate level in yeast cells exposed to heat stress, indicating that these residues are also crucial for its physiological functions. These studies provide some benefits of Mpr1 applications, such as the breeding of industrial yeasts and the development of antifungal drugs."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420845751167600512","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"90708116"},{"@type":"NRID","@value":"1000090708116"},{"@type":"NRID","@value":"9000398839554"},{"@type":"NRID","@value":"9000413774956"},{"@type":"NRID","@value":"9000318156830"},{"@type":"NRID","@value":"9000413774959"},{"@type":"NRID","@value":"9000409330925"},{"@type":"NRID","@value":"9000397842085"},{"@type":"NRID","@value":"9000019198447"},{"@type":"NRID","@value":"9000291273195"},{"@type":"NRID","@value":"9000299859266"},{"@type":"NRID","@value":"9000414332310"},{"@type":"NRID","@value":"9000413774935"},{"@type":"NRID","@value":"9000317166762"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/r-nasuno"}],"foaf:name":[{"@language":"en","@value":"Nasuno, Ryo"}]},{"@id":"https://cir.nii.ac.jp/crid/1420282801187370112","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"50452529"},{"@type":"NRID","@value":"1000050452529"},{"@type":"NRID","@value":"9000016864275"},{"@type":"NRID","@value":"9000398156370"},{"@type":"NRID","@value":"9000001750956"},{"@type":"NRID","@value":"9000365497405"},{"@type":"NRID","@value":"9000317166763"},{"@type":"NRID","@value":"9000398801626"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/strb"}],"foaf:name":[{"@language":"en","@value":"Hirano, 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Hiroshi"}]}],"publication":{"publicationIdentifier":[{"@type":"ISSN","@value":"10916490"},{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"},{"@type":"NCID","@value":"AA11726874"}],"prism:publicationName":[{"@language":"en","@value":"Proceedings of the National Academy of Sciences of the United States of America"}],"dc:publisher":[{"@value":"National Academy of Sciences"}],"prism:publicationDate":"2013-07-01","prism:volume":"110","prism:number":"29","prism:startingPage":"11821","prism:endingPage":"11826"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["Copyright c 2013 National Academy of Sciences"],"url":[{"@id":"https://naist.repo.nii.ac.jp/records/9107"},{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.1300558110"},{"@id":"http://hdl.handle.net/10061/8821"}],"foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=cyclic%20amine%20N-acetyltransferase","dc:title":"cyclic amine N-acetyltransferase"},{"@id":"https://cir.nii.ac.jp/all?q=X-ray%20crystallography","dc:title":"X-ray crystallography"},{"@id":"https://cir.nii.ac.jp/all?q=reaction%20mechanism","dc:title":"reaction mechanism"},{"@id":"https://cir.nii.ac.jp/all?q=antioxidant%20enzyme","dc:title":"antioxidant enzyme"}],"dcterms:subject":[{"subjectScheme":"Other","notation":[{"@language":"en","@value":"cyclic amine N-acetyltransferase"}]},{"subjectScheme":"Other","notation":[{"@language":"en","@value":"X-ray crystallography"}]},{"subjectScheme":"Other","notation":[{"@language":"en","@value":"reaction mechanism"}]},{"subjectScheme":"Other","notation":[{"@language":"en","@value":"antioxidant enzyme"}]}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040000782102612096","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"22121002"},{"@type":"JGN","@value":"JP22121002"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PLANNED-22121002/"}],"notation":[{"@language":"ja","@value":"動物・植物細胞のシグナル検知と伝達の構造生物学"},{"@language":"en","@value":"Structural biology of animal and plant signaling proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1040000782183993984","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"23770119"},{"@type":"JGN","@value":"JP23770119"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-23770119/"}],"notation":[{"@language":"ja","@value":"ミオシンによる選択的積み荷輸送機構の構造的研究"},{"@language":"en","@value":"Structural study of slective cargo transport by unconventional myosins"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282257233110656","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"25440025"},{"@type":"JGN","@value":"JP25440025"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-25440025/"}],"notation":[{"@language":"ja","@value":"高等植物の根の形態形成を制御する新規転写制御機構の構造的研究"},{"@language":"en","@value":"Structural study of the novel transcription mechanism essential for root development of higher plants"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050858784329485184","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Enhancement of the proline and nitric oxide synthetic pathway improves fermentation ability under multiple baking-associated stress conditions in industrial baker's yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002215924168320","@type":"Article","resourceType":"学術雑誌論文(journal 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