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.

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。 金属和金属蛋白对于许多细胞过程至关重要。 我们的实验室使用大分子X射线晶体学来研究金属蛋白的结构和功能。 这些蛋白质包括调节细胞镍摄取的DNA结合蛋白NIKR镍调节转录因子NIKR。从生物素生物合成酶（BIOB）和丙酮酸甲酸甲酸甲酸酯酶（PFL）激活酶（PFLAE）涉及的自由基S-腺苷甲硫代氨酸（SAM）酶生物素合酶（BIOB），通过形成蛋白质的gllycyl radical on Pfl;和羟丙基膦酸环氧酶（HPPE），它使用单核铁位点在形成抗生素fosfymycin时催化独特的环氧化。我们已经解决了所有这些蛋白质的初始晶体结构并发表，其中一些工作先前是在SSRL上进行的。现在，我们正在追求这些金属酶在多个状态中的进一步晶体学表征，以更充分地了解它们的功能特性。