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: 8362216
• 负责人: PETER GOLDMAN
• 金额: $ 0.03万
• 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/8362216
• 关键词: Acids; Anabolism; Antibiotics; Biotin; Cell physiology; DNA-Binding Proteins; Enzymes; Fosfomycin; Funding; Grant; Iron; Laboratories; Metabolism; Metalloproteins; Metals; Mononuclear; National Center for Research Resources; Nickel; Principal Investigator; Property; Protein Binding; Proteins; Publishing; Radiation; Research; Research Infrastructure; Resources; S-Adenosylmethionine; Site; Source; Structure; United States National Institutes of Health; Work; X-Ray Crystallography; biotin synthase; cost; epoxidase; formate C-acetyltransferase; formate acetyltransferase activating enzyme; metalloenzyme; structural biology; transcription factor; uptake

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. 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.

这个子项目是利用这些资源的众多研究子项目之一