CRYO-EM OF AN OCTOMERIC FORM OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE

八聚体丙酮酸：铁氧还蛋白氧化还原酶的冷冻电镜

• 批准号: 7956446
• 负责人: ROBERT M GLAESER
• 金额: $ 0.65万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-05-01 至 2010-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7956446
• 关键词: Address; Computer Retrieval of Information on Scientific Projects Database; Desulfovibrio africanus; Desulfovibrio vulgaris; Enzymes; Funding; Grant; Institution; Microscopy; Molecular; Multienzyme Complexes; Play; Pyruvate synthase; Research; Research Personnel; Resolution; Resources; Role; Source; Structure; United States National Institutes of Health; dimer; nanometer

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. Pyruvate:ferredoxin oxidoreductase (PFOR) exists as a dimer in Desulfovibrio africanus, but as an octomer (MW > 1 MDa) in Desulfovibrio vulgaris. The question that this project will address is whether there are observable shifts in the helix packing when the two structures are compared at sub-nanometer resolution. The structural comparison of dimeric and octomeric complexes of this enzyme is expected to play an important role in understanding why it has proven to be biochemically more advantageous for D.vulgaris to assemble PFOR as an octomer while the dimeric form of the enzyme is better suited for D. africanus.

这个子项目是众多研究子项目之一