CRYSTALLOGRAPHIC STUDIES OF METALLOPROTEINS (NIKR, BIOB, PFLAE, AND HPPE)

金属蛋白的晶体学研究（NIKR、BIOB、PFLAE 和 HPPE）

• 批准号: 8170177
• 负责人: PETER GOLDMAN
• 金额: $ 0.41万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170177
• 关键词: Acids; Anabolism; Antibiotics; Biotin; Cell physiology; Computer Retrieval of Information on Scientific Projects Database; DNA-Binding Proteins; Enzymes; Fosfomycin; Funding; Grant; Institution; Iron; Laboratories; Metabolism; Metalloproteins; Metals; Mononuclear; Nickel; Property; Protein Binding; Proteins; Publishing; Research; Research Personnel; Resources; Site; Source; Structure; United States National Institutes of Health; Work; X-Ray Crystallography; biotin synthase; epoxidase; formate C-acetyltransferase; formate acetyltransferase activating enzyme; metalloenzyme; transcription factor; uptake

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. Metals and metalloproteins are essential for many cellular processes. Our laboratory uses macromolecular X-ray crystallography to study the structure and function of metalloproteins. These proteins include nickel regulatory transcription factor NikR, a DNA-binding protein that regulates cellular nickel uptake; the radical S-adenosylmethionine (SAM) enzymes biotin synthase (BioB), involved in biotin biosynthesis, and pyruvate formate-lyase (PFL) activating enzyme (PflAE), involved in anaerobic metabolism by formation of a protein bound glycyl radical on PFL; and hydroxypropylphosphonic acid epoxidase (HppE), which uses a mononuclear iron site to catalyze a unique epoxidation in the formation of the antibiotic fosfomycin. We have solved and published initial crystal structures of all of these proteins, and some of this work was carried out previously at SSRL. We are now in pursuit of further crystallographic characterization of these metalloenzymes in multiple states to more fully understand their functional properties.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 金属和金属蛋白是许多细胞过程所必需的。 本实验室使用大分子X射线晶体学来研究金属蛋白的结构和功能。 这些蛋白质包括镍调节转录因子NikR，一种调节细胞镍吸收的DNA结合蛋白;自由基S-腺苷甲硫氨酸（SAM）酶生物素合酶（BioB），参与生物素生物合成，和丙酮酸甲酸裂解酶（PFL）激活酶（PflAE），通过在PFL上形成蛋白质结合的甘氨酰自由基参与厌氧代谢;和羟丙基膦酸环氧酶（HppE），其使用单核铁位点来催化抗生素磷霉素形成中的独特环氧化。我们已经解决并公布了所有这些蛋白质的初始晶体结构，其中一些工作以前在SSRL进行。我们现在正在追求这些金属酶在多种状态下的进一步晶体学表征，以更全面地了解它们的功能特性。