MECHANISM OF IRON STORAGE BY BLOOM-FORMING PENNATE DIATOMS

开花羽状硅藻储铁机制

• 批准号: 8362419
• 负责人: MICHAEL MURPHY
• 金额: $ 0.06万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362419
• 关键词: Amino Acids; Carbon; Ceruloplasmin; Characteristics; Data; Diatoms; Ferritin; Funding; Grant; Iron; Mammals; Marines; Metals; Minerals; National Center for Research Resources; Oceans; Organism; Pathway interactions; Plants; Play; Principal Investigator; Production; Proteins; Radiation; Research; Research Infrastructure; Resources; Role; Site; Source; Structure; United States National Institutes of Health; Variant; Zinc; cost; insight; microorganism; novel; research study; structural biology

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. Ferritins are a broad superfamily of iron storage and detoxifying proteins found in plants, mammals and many microorganisms. A novel ferritin was found in marine pennate diatoms, unicellular photosynthetic organisms that play a major role in global primary production and carbon sequestration in the deep ocean. Crystal structures of ferritin derived from the pennate diatom Pseudo-nitzschia multiseries (PmFTN) revealed the characteristic ferritin ferroxidase centres, monomeric fold and spherical assembly. Three metal sites (A, B, C) were identified from iron(II) and zinc(II) crystal soaking experiments and anomalous dispersion data. The observed iron and zinc atoms form a pathway leading towards the central cavity where the stored iron mineral is formed. Metal coordinating residues are hypothesized to gate the passage of iron from the ferroxidase site to nucleate the mineral core. We will determine crystal structures of variants of metal coordinating amino acids in the presence of iron(II) and to gain further insights into the iron storage mechanism of PmFTN.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的主要研究者可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 铁蛋白是植物、哺乳动物和许多微生物中发现的一个广泛的铁储存和解毒蛋白质超家族。在海洋羽状硅藻中发现了一种新型铁蛋白，这种单细胞光合生物在全球初级生产和深海碳封存中发挥着重要作用。源自羽状硅藻拟菱形藻多系 (PmFTN) 的铁蛋白晶体结构揭示了特征性铁蛋白亚铁氧化酶中心、单体折叠和球形组装。根据铁（II）和锌（II）晶体浸泡实验和反常色散数据确定了三个金属位点（A、B、C）。观察到的铁和锌原子形成一条通向中央空腔的通道，在那里形成储存的铁矿物。假设金属配位残基可控制铁从亚铁氧化酶位点到使矿物核心成核的通道。我们将确定铁 (II) 存在下金属配位氨基酸变体的晶体结构，并进一步了解 PmFTN 的铁储存机制。