SMALL ANGLE X-RAY SCATTERING OF F FACTOR TRAI AND ITS DOMAINS

F因子TRAI及其域的小角X射线散射

• 批准号: 8363565
• 负责人: JOEL F SCHILDBACH
• 金额: $ 1.04万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-07-01 至 2012-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363565
• 关键词: C-terminal; Cleaved cell; DNA Binding; Data; F Factor; Funding; Grant; N-terminal; National Center for Research Resources; Plasmids; Principal Investigator; Process; Proteins; Relative (related person); Research; Research Infrastructure; Resources; Roentgen Rays; Shapes; Source; Structure; United States National Institutes of Health; cost; helicase; polypeptide; research study

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. TraI, a protein from the conjugative plasmid F factor, is essential for the plasmid transfer process. The protein includes a relaxase activity that cleaves one plasmid strand prior to transfer, and a helicase activity ---- both of which must be in one polypeptide chain for efficient conjugative transfer. We have determined the crystal structure of the relaxase domain (the N-terminal 36 kDa of the 192 kDa protein), and are near solving the 3D NMR structure of a second 20 kDa region. The C-terminal domain has been solved, and we are pursuing structures of other domains. We want to collect SAXS data to determine the shape of the intact protein and various fragments, and attempt to fit the regions of known structure into the resulting shapes. The experiments will provide information on the orientation of the domains relative to each other and whether the orientation of the domains changes upon DNA binding.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 TraI是一种来自接合性质粒F因子的蛋白质，对于质粒转移过程至关重要。 该蛋白质包括在转移前裂解一条质粒链的松弛酶活性和解旋酶活性，这两种活性必须在一条多肽链中才能进行有效的接合转移。 我们已经确定了松弛酶结构域的晶体结构（192 kDa蛋白质的N-末端36 kDa），并接近解决第二个20 kDa区域的3D NMR结构。 C-末端结构域已经解决，我们正在研究其他结构域的结构。 我们希望收集SAXS数据来确定完整蛋白质和各种片段的形状，并尝试将已知结构的区域拟合到所得形状中。 实验将提供关于结构域相对于彼此的取向以及结构域的取向是否在DNA结合时改变的信息。