ATOMIC RESOLUTION STUDIES OF FERREDOXIN FROM HALOARCULA MARISMORTUI

海纹藻铁氧还蛋白的原子分辨率研究

• 批准号: 6339131
• 负责人: FELIX FROLOW
• 金额: $ 0.46万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-08-15 至 2001-08-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6339131
• 关键词: bioimaging /biomedical imaging; biological products; biomedical resource; proteins; radiography; structural biology

The research in my lab has focused on the structure determination of (i) bacterial channel-forming toxins, such as Staphylococcal leukocidin (LukF) and (ii) the ligand binding domain of ligand gated ion channels. Data from the F2 beamline has enabled us to solve the structure of the water-soluble form of LukF and the ligand binding domain of the GluR2, AMPA-selective glutamate receptor. Both structures were solved by MAD phasing from selenomethionine crystals at ~2.3 A resolution. Presently, both structures have been refined and we are currently in the process of manuscript preparation. From these structures we have furthered our understanding, at the molecular level, of the conformational changes that bacterial toxins undergo as a consequence of membrane binding and oligomerization and we have provided, for the first time, a view of the extracellular domain of a ligand gated ion channel.

我实验室的研究重点是结构测定 (i) 细菌通道形成毒素，例如葡萄球菌 杀白细胞素 (LukF) 和 (ii) 配体门控的配体结合结构域 离子通道。 来自 F2 光束线的数据使我们能够解决 LukF 水溶性形式的结构和配体结合 GluR2 的结构域，AMPA 选择性谷氨酸受体。 两个都 通过 MAD 定相从硒代蛋氨酸晶体中解析出结构 分辨率约为 2.3 A。 目前，两种结构均已完善 我们目前正在准备稿件。 从 这些结构我们在分子水平上进一步加深了理解 水平，细菌毒素经历的构象变化 膜结合和寡聚化的结果，我们有 首次提供了细胞外结构域的视图 配体门控离子通道。