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.

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。 丙酮酸：铁氧还氧化还原酶（PFOR）作为desulfovibrio Africanus的二聚体存在，但在Desulfovibrio vulgaris中作为Octomer（MW> 1 MDA）。该项目将解决的问题是，当两个结构以亚纳米分辨率进行比较时，螺旋堆积是否有可观察到的变化。 预计该酶的二聚体和八体复合物的结构比较在理解为什么D.Vulgaris将PFOR作为Octomer组装成Octomer而在生物化学上具有重要作用，而该酶的二聚体形式更适合D.非洲人。