Department of Dermatology, People's Hospital of SND, Suzhou, Jiangsu 215129, People's Republic of China.
Key Laboratory of Cell Differentiation and Apoptosis of The Chinese Ministry of Education, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, People's Republic of China.
Acta Crystallogr F Struct Biol Commun. 2022 Sep 1;78(Pt 9):324-329. doi: 10.1107/S2053230X22007919. Epub 2022 Aug 22.
Chickpea is a crop that is known as a source of high-quality proteins. CL-AI, which belongs to the 11S globulin and cupin superfamily, was initially identified in chickpea seeds. CL-AI has recently been shown to inhibit various types of α-amylases. To determine its molecular mechanism, the crystal structure of CL-AI was solved at a final resolution of 2.2 Å. Structural analysis indicated that each asymmetric unit contains three molecules with threefold symmetry and a head-to-tail association, and each molecule is divided into an α-chain and a β-chain. CL-AI has high structural similarity to other 11S globulins and canonical metal-dependent enzyme-related cupin proteins, whereas its stimilarity to α-amylase inhibitor from Phaseolus vulgaris is quite low. The structure presented here will provide insight into the function of CL-AI.
鹰嘴豆是一种已知的高蛋白作物。CL-AI 最初在鹰嘴豆种子中被鉴定出来，属于 11S 球蛋白和 cupin 超家族。最近的研究表明，CL-AI 可以抑制多种类型的 α-淀粉酶。为了确定其分子机制，我们解析了 CL-AI 的晶体结构，最终分辨率为 2.2 Å。结构分析表明，每个不对称单元包含三个具有三进制对称和头尾结合的分子，每个分子分为α-链和β-链。CL-AI 与其他 11S 球蛋白和典型的金属依赖性酶相关 cupin 蛋白具有高度的结构相似性，而与菜豆的 α-淀粉酶抑制剂的相似性则相当低。本文所提供的结构将为 CL-AI 的功能提供深入的了解。
