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Crystallization and crystallographic studies of a novel chickpea 11S globulin.

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.

SUBMITTER: Sun L

PROVIDER: S-EPMC9435671 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature

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Crystallization and crystallographic studies of a novel chickpea 11S globulin.

Sun Linan L Zhou Aiwu A Zhang Fei F

Acta crystallographica. Section F, Structural biology communications 20220822 Pt 9

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, an ...[more]

PMID: 36048082

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