{"title":"番茄花叶病毒抗性蛋白 Tm-1 的抑制结构域的结晶和初步 X 射线晶体学分析。","authors":"Masahiko Kato, Yuichiro Kezuka, Chihoko Kobayashi, Kazuhiro Ishibashi, Takamasa Nonaka, Masayuki Ishikawa, Estuko Katoh","doi":"10.1107/S1744309113030819","DOIUrl":null,"url":null,"abstract":"<p><p>Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of Tm-1 are reported. A three-wavelength MAD data set was collected from a selenomethionine-labelled crystal and processed to 2.7 Å resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.</p>","PeriodicalId":7310,"journal":{"name":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","volume":null,"pages":null},"PeriodicalIF":0.9000,"publicationDate":"2013-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3855732/pdf/","citationCount":"0","resultStr":"{\"title\":\"Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.\",\"authors\":\"Masahiko Kato, Yuichiro Kezuka, Chihoko Kobayashi, Kazuhiro Ishibashi, Takamasa Nonaka, Masayuki Ishikawa, Estuko Katoh\",\"doi\":\"10.1107/S1744309113030819\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of Tm-1 are reported. A three-wavelength MAD data set was collected from a selenomethionine-labelled crystal and processed to 2.7 Å resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.</p>\",\"PeriodicalId\":7310,\"journal\":{\"name\":\"Acta Crystallographica Section F-structural Biology and Crystallization Communications\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.9000,\"publicationDate\":\"2013-12-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3855732/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta Crystallographica Section F-structural Biology and Crystallization Communications\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1107/S1744309113030819\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2013/11/29 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta Crystallographica Section F-structural Biology and Crystallization Communications","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1107/S1744309113030819","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2013/11/29 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
Tm-1是番茄花叶病毒RNA复制的抑制蛋白,含有两个保守结构域:N-端为未定性结构域,C-端为TIM-桶状结构域。Tm-1 的 N 端结构域具有抑制活性,但其三维结构尚未确定。本文报告了 Tm-1 N 端结构域的结晶和初步 X 射线衍射。从硒代蛋氨酸标记的晶体中收集了三波长 MAD 数据集,并将其处理为 2.7 Å 分辨率。该晶体属于三菱空间群 P1,单位晶胞参数为 a = 77.97、b = 105.28、c = 110.62 Å、α = 94.6、β = 109.3、γ = 108.0°。
Crystallization and preliminary X-ray crystallographic analysis of the inhibitory domain of the tomato mosaic virus resistance protein Tm-1.
Tm-1, an inhibitor protein of Tomato mosaic virus RNA replication, contains two conserved domains: an uncharacterized domain at its N-terminus and a TIM-barrel-like domain at its C-terminus. The N-terminal domain of Tm-1 has an inhibitory activity and its three-dimensional structure has not been determined. Here, the crystallization and preliminary X-ray diffraction of the N-terminal domain of Tm-1 are reported. A three-wavelength MAD data set was collected from a selenomethionine-labelled crystal and processed to 2.7 Å resolution. The crystal belonged to the triclinic space group P1, with unit-cell parameters a = 77.97, b = 105.28, c = 110.62 Å, α = 94.6, β = 109.3, γ = 108.0°.
期刊介绍:
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