ULTRA-HIGH RESOLUTION STRUCTURES OF THE SRP GTPASE AND ITS HETERODIMERIC RECEPTO

SRP GTPase 及其异二聚体受体的超高分辨率结构

• 批准号: 7597906
• 负责人: Douglas M. Freymann
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597906
• 关键词: Complex; Computer Retrieval of Information on Scientific Projects Database; Condition; Crystallization; Data; Data Collection; Exhibits; Funding; Future; Grant; Guanosine Diphosphate; Guanosine Triphosphate Phosphohydrolases; Institution; Mediating; Molecular; Numbers; Play; Property; Proteins; Research; Research Personnel; Resources; Role; Signal Recognition Particle; Source; Structural Protein; Structure; Thermus; Time; United States National Institutes of Health; base; member; mouse Gdi2 protein; novel; receptor; ultra high resolution

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This proposal has two aims: the first is completion of ultra-high resolution data collection from the GDP and GMPPNP complexes of the SRP GTPase, Ffh, from Thermus aquaticus. These structures, with data from crystals of the apo protein previously collected at SSRL, will form the basis for a comparitive analysis of the structural states of Ffh at ultra-high resolution. Although a member of the GTPase superfamily, the SRP GTPase exhibits a number of novel properties that we aim to understand at a protein structural level. In addition, we have estabished preliminary conditions for crystallization of the GTP-dependent complex of the SRP GTPase Ffh with its receptor FtsY, also a GTPase. We anticipate optimization of the crystallization conditions in the near future, and are requesting data collection time in order to determine this structure using MAD. The structure of the Ffh/FtsY NG complex is particularly significant, because it will reveal the structural basis for the molecular 'handshake' that plays a central role in SRP-mediated targeting.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 这项建议有两个目标：第一个目标是完成对水生黄热菌SRP GTPase FFH的GDP和GMPPNP复合体的超高分辨率数据收集。这些结构，以及以前在SSRL收集的载脂蛋白晶体的数据，将形成以超高分辨率比较分析FFH结构状态的基础。虽然SRP GTPase是GTPase超家族的一员，但它表现出许多我们希望在蛋白质结构水平上理解的新特性。此外，我们还为SRP GTP酶FFH与其受体FtsY(也是一种GTP酶)的依赖GTP的复合体的结晶建立了初步的条件。我们预计在不久的将来结晶条件将得到优化，并要求获得数据收集时间，以便使用MAD确定该结构。FFH/FtsY NG复合体的结构特别重要，因为它将揭示在SRP介导的靶向中发挥核心作用的分子“握手”的结构基础。