5gyl
From Proteopedia
Structure of Cicer arietinum 11S gloubulin
Structural highlights
Publication Abstract from PubMedChickpea 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 alpha-amylases. To determine its molecular mechanism, the crystal structure of CL-AI was solved at a final resolution of 2.2 A. 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 alpha-chain and a beta-chain. CL-AI has high structural similarity to other 11S globulins and canonical metal-dependent enzyme-related cupin proteins, whereas its stimilarity to alpha-amylase inhibitor from Phaseolus vulgaris is quite low. The structure presented here will provide insight into the function of CL-AI. Crystallization and crystallographic studies of a novel chickpea 11S globulin.,Sun L, Zhou A, Zhang F Acta Crystallogr F Struct Biol Commun. 2022 Sep 1;78(Pt 9):324-329. doi: , 10.1107/S2053230X22007919. Epub 2022 Aug 22. PMID:36048082[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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