Crystallization and crystallographic studies of a novel chickpea 11S globulin

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.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: 11S globulins chickpeas crystal structure cupin proteins CL-AI research communications Source Type: research