5GYL
Structure of Cicer arietinum 11S gloubulin
5GYL の概要
| エントリーDOI | 10.2210/pdb5gyl/pdb |
| 分子名称 | legumin-like protein (2 entities in total) |
| 機能のキーワード | 11s gloubulin, seeds, plant protein |
| 由来する生物種 | Cicer arietinum |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 162735.36 |
| 構造登録者 | |
| 主引用文献 | Sun, L.,Zhou, A.,Zhang, F. Crystallization and crystallographic studies of a novel chickpea 11S globulin. Acta Crystallogr.,Sect.F, 78:324-329, 2022 Cited by PubMed Abstract: 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. PubMed: 36048082DOI: 10.1107/S2053230X22007919 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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