Determination of whole complex structure of decarboxylase sodium pump

脱羧酶钠泵整体复合结构的测定

• 批准号: 24770100
• 负责人: INOUE Michio
• 金额: $ 3万
• 依托单位: Tohoku University (2013)Kyushu University (2012)
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (B)
• 财政年份: 2012
• 资助国家: 日本
• 起止时间: 2012-04-01 至 2014-03-31
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-24770100/
• 关键词: 膜タンパク質; X線結晶構造解析; 膜タンパク質複合体の結晶構造解析

The oxaloacetate decarboxylase primary Na+ pump complex (OAD) functions in energy generation for the surviving of some pathogenic bacteria under anaerobic conditions. OAD composes of three subunits: OAD-alpha, OAD-beta and OAD-gamma. Each subunit is characterized but the mechanism of OAD as a whole complex remains still unclear. The determination of the whole complex of OAD is expected to reveal not only the molecular mechanism of the energetic coupling but also the stoichiometry of subunits. At the initial stage of structural analysis, a purification of stable and high quality proteins is required. Here it is reported that we succeeded in purification of high quality Oad2 complex for structural analysis and it is suggested that the stoichiometry of OAD subunits is 4:2:2 instead of 1:1:1.

草酰乙酸脱羧酶初级 Na+ 泵复合物 (OAD) 的作用是产生能量，以维持某些病原菌在厌氧条件下的生存。 OAD 由三个亚基组成：OAD-α、OAD-β 和 OAD-gamma。每个亚基都有其特征，但 OAD 作为一个整体复合体的机制仍不清楚。 OAD整个复合物的测定不仅有望揭示能量耦合的分子机制，还能揭示亚基的化学计量。在结构分析的初始阶段，需要纯化稳定且高质量的蛋白质。据报道，我们成功纯化了高质量的Oad2复合物进行结构分析，并建议OAD亚基的化学计量为4:2:2而不是1:1:1。

项目成果

Radically Different Thioredoxin Domain Arrangement of ERp46, an Efficient Disulfide Bond Introducer of the Mammalian PDI Family

• DOI: 10.1016/j.str.2013.12.013
• 发表时间: 2014-03-04
• 期刊: STRUCTURE
• 影响因子: 5.7
• 作者: Kojima, Rieko;Okumura, Masaki;Inaba, Kenji
• 通讯作者: Inaba, Kenji