Surya V S R K Pulavarti, Yunfen He, Erik A Feldmann, Alexander Eletsky, Thomas B Acton, Rong Xiao, John K Everett, Gaetano T Montelione, Michael A Kennedy, Thomas Szyperski
{"title":"溶液核磁共振结构提供了大蛋白结构域家族PF08369的第一个结构覆盖和暗作用原叶绿素内酯氧化还原酶复合物的互补结构覆盖。","authors":"Surya V S R K Pulavarti, Yunfen He, Erik A Feldmann, Alexander Eletsky, Thomas B Acton, Rong Xiao, John K Everett, Gaetano T Montelione, Michael A Kennedy, Thomas Szyperski","doi":"10.1007/s10969-013-9159-5","DOIUrl":null,"url":null,"abstract":"<p><p>High-quality NMR structures of the C-terminal domain comprising residues 484-537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9-61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhibit a mixed α/β fold comprised of three α-helices and a small β-sheet packed against second α-helix. These two proteins share 29% sequence similarity and their structures are globally quite similar. The structures of BchB(484-537) and Asr4154(9-61) are the first representative structures for the large protein family (Pfam) PF08369, a family of unknown function currently containing 610 members in bacteria and eukaryotes. Furthermore, BchB(484-537) complements the structural coverage of the dark-operating protochlorophyllide oxidoreductase.</p>","PeriodicalId":73957,"journal":{"name":"Journal of structural and functional genomics","volume":"14 3","pages":"119-26"},"PeriodicalIF":0.0000,"publicationDate":"2013-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s10969-013-9159-5","citationCount":"1","resultStr":"{\"title\":\"Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes.\",\"authors\":\"Surya V S R K Pulavarti, Yunfen He, Erik A Feldmann, Alexander Eletsky, Thomas B Acton, Rong Xiao, John K Everett, Gaetano T Montelione, Michael A Kennedy, Thomas Szyperski\",\"doi\":\"10.1007/s10969-013-9159-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>High-quality NMR structures of the C-terminal domain comprising residues 484-537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9-61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhibit a mixed α/β fold comprised of three α-helices and a small β-sheet packed against second α-helix. These two proteins share 29% sequence similarity and their structures are globally quite similar. The structures of BchB(484-537) and Asr4154(9-61) are the first representative structures for the large protein family (Pfam) PF08369, a family of unknown function currently containing 610 members in bacteria and eukaryotes. Furthermore, BchB(484-537) complements the structural coverage of the dark-operating protochlorophyllide oxidoreductase.</p>\",\"PeriodicalId\":73957,\"journal\":{\"name\":\"Journal of structural and functional genomics\",\"volume\":\"14 3\",\"pages\":\"119-26\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/s10969-013-9159-5\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of structural and functional genomics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/s10969-013-9159-5\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2013/8/21 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of structural and functional genomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/s10969-013-9159-5","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2013/8/21 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes.
High-quality NMR structures of the C-terminal domain comprising residues 484-537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9-61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhibit a mixed α/β fold comprised of three α-helices and a small β-sheet packed against second α-helix. These two proteins share 29% sequence similarity and their structures are globally quite similar. The structures of BchB(484-537) and Asr4154(9-61) are the first representative structures for the large protein family (Pfam) PF08369, a family of unknown function currently containing 610 members in bacteria and eukaryotes. Furthermore, BchB(484-537) complements the structural coverage of the dark-operating protochlorophyllide oxidoreductase.
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