Crystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters,FEBS Letters

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Crystal structure of the rice acyl‐CoA‐binding protein OsACBP2 in complex with C18:3‐CoA reveals a novel pattern of binding to acyl‐CoA esters
FEBS Letters ( IF 3.0 ) Pub Date : 2020-09-18 , DOI: 10.1002/1873-3468.13923
Jing Jin ₁ , Ze-Hua Guo ₂ , Quan Hao ₁ , Mee-Len Chye _{2,

3}

Affiliation

Acyl‐CoA‐binding proteins (ACBPs) are a family of proteins that bind acyl‐CoA esters at a conserved acyl‐CoA‐binding domain. ACBPs maintain intracellular acyl‐CoA pools to regulate lipid metabolism. Here, we report on the structure of rice OsACBP2 in complex with C18:3‐CoA ester. The residues Y33, K34 and K56 of OsACBP2 play a crucial role in binding the CoA group, while residues N23, L27, K52 and Y55 in one molecule of OsACBP2 cooperate with L27, L28, A59 and A62 from another anchoring the fatty acyl group. Multiangle light scattering assays indicate that OsACBP2 binds C18:3‐CoA as a monomer. The first complex structure of a plant ACBP binding with C18:3‐CoA is therefore presented, providing a novel model for the interaction between an acyl‐CoA ester and the acyl‐CoA‐binding domain(s).

中文翻译：

与 C18:3-CoA 复合的水稻酰基辅酶 A 结合蛋白 OsACBP2 的晶体结构揭示了与酰基辅酶 A 酯结合的新模式

酰基辅酶A结合蛋白（ACBPs）是在保守的酰基辅酶A结合域结合酰基辅酶A酯的蛋白质家族。ACBP 维持细胞内酰基辅酶 A 池以调节脂质代谢。在这里，我们报告了与 C18:3-CoA 酯复合的水稻 OsACBP2 的结构。OsACBP2 的 Y33、K34 和 K56 残基在结合 CoA 基团中起关键作用，而一个 OsACBP2 分子中的 N23、L27、K52 和 Y55 残基与另一个锚定脂肪酰基的分子中的 L27、L28、A59 和 A62 协同作用。多角度光散射分析表明 OsACBP2 作为单体结合 C18:3-CoA。因此，提出了与 C18:3-CoA 结合的植物 ACBP 的第一个复杂结构，为酰基辅酶 A 酯与酰基辅酶 A 结合域之间的相互作用提供了一个新模型。

更新日期：2020-09-18

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