BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF MERCURIC ION REDUCTASE

汞离子还原酶的生化和结构表征

• 批准号: 8170506
• 负责人: Susan Mary Miller
• 金额: $ 0.71万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 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/8170506
• 关键词: Alkylmercury lyase; Amino Acids; Binding; Binding Proteins; Biochemical; Catalysis; Catalytic Domain; Chimera organism; Complex; Computer Retrieval of Information on Scientific Projects Database; Disulfides; Docking; Drug Metabolic Detoxication; Family; Funding; Glutathione Reductase; Grant; Institution; Ions; Kinetics; Membrane Transport Proteins; Mercury; Metals; Molecular Weight; Mutagenesis; N-terminal; Oxidoreductase; Pathway interactions; Proteins; Research; Research Personnel; Resources; Sequence Homology; Site; Source; Structure; Thioredoxin; United States National Institutes of Health; protein protein interaction; pyridine nucleotide

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 project focuses on the structural and kinetic characterization of mercuric ion reductase. Mercuric ion reductase is composed of two domains, a catalytic core domain that is highly homologous to the FAD containing pyridine nucleotide disulfide reductase family i.e. glutathione reductase and a second domain, a ~69 amino acid N-terminal domain, with sequence homology to metal binding proteins. We are focusing on two aspects: 1) characterization of structural features in the Hg(II) binding pathway that are essential for efficient catalysis and 2) elucidating mechanisms of protein/protein interactions between the catalytic core of MerA and the NmerA domain as well as of core with other proteins of the mercury detoxification pathway including MerB, an organomercurial lyase, and the integral membrane transport proteins, MerT or MerC. We use Chimera to graphically present structures of Hg(II) and other complexes of the catalytic core domain alone and interacting with other small molecular weight proteins like NmerA or thioredoxin. In addition, we use Chimera to assist us in evaluating sites for mutagenesis and examining possible modes for docking between MerA and the other mer pathway proteins.

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。 该项目着重于汞离子还原酶的结构和动力学表征。 汞离子还原酶由两个结构域组成，这是一种催化核心结构域，与含有吡啶核苷酸二硫化物还原酶家族的FAD高度同源，即谷胱甘肽还原酶和第二个结构域，A〜69氨基酸N末端结构域，具有与金属结合蛋白的序列同源的序列。 We are focusing on two aspects: 1) characterization of structural features in the Hg(II) binding pathway that are essential for efficient catalysis and 2) elucidating mechanisms of protein/protein interactions between the catalytic core of MerA and the NmerA domain as well as of core with other proteins of the mercury detoxification pathway including MerB, an organomercurial lyase, and the integral membrane transport proteins, MerT or merc。 我们使用嵌合体来图形地呈现Hg（II）的结构和单独催化核心结构域的其他复合物，并与其他小的分子量蛋白（如NMERA或硫氧还蛋白）相互作用。 此外，我们使用嵌合体来帮助我们评估诱变的位点，并检查Mera与其他MER途径蛋白之间的可能对接模式。