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

这个子项目是许多利用 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。 丙酮酸：铁氧还蛋白氧化还原酶（PFOR）在非洲脱硫弧菌中以二聚体形式存在，而在普通脱硫弧菌中以八聚体形式存在（MW > 1 MDa）。这个项目将解决的问题是，当两种结构在亚纳米分辨率下进行比较时，螺旋包装中是否有可观察到的变化。 这种酶的二聚体和八聚体复合物的结构比较，预计将发挥重要作用，在理解为什么它已被证明是生物化学更有利的D.寻常组装PFOR作为八聚体，而二聚体形式的酶更适合D.非洲人

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.