TERTIARY AND QUATERNARY STRUCTURE CHARACTERIZATION OF METALLOENZYMES IN SOLUTION

溶液中金属酶的三级和四级结构表征

• 批准号: 8171518
• 负责人: CATHERINE L DRENNAN
• 金额: $ 1.43万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-07-01 至 2011-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171518
• 关键词: Bacteria; Computer Retrieval of Information on Scientific Projects Database; Cytochromes; Electron Transport; Funding; Grant; Heme; Institution; Proteins; Radial; Research; Research Personnel; Resolution; Resources; Shewanella; Solutions; Source; Structure; United States National Institutes of Health; metalloenzyme

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. MtrA is a 10-heme cytochrome from the bacteria, Shewanella oneidensis. No crystal structure yet exists for this protein. A recently proposed hypothesis suggests that it is a highly asymmetric protein with an aspect ratio of ~ 4:1, which would allow parallel stacking of the hemes. Determination of its radius of gyration and low-resolution solution structure with SAXS will allow us to investigate this hypothesis and further understand the mechanism of electron transfer in this protein.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 MTRA是细菌Shewanella Oneidensis的10血红素细胞色素。该蛋白质尚无晶体结构。最近提出的假设表明，它是一种高度不对称的蛋白质，纵横比为〜4：1，可以平行地堆叠下摆。用SAXS确定其回旋的半径和低分辨率溶液结构将使我们能够研究该假设，并进一步了解该蛋白质中电子转移的机制。