5GYL

Structure of Cicer arietinum 11S gloubulin

Summary for 5GYL

• Entry DOI: 10.2210/pdb5gyl/pdb
• Descriptor: legumin-like protein (2 entities in total)
• Functional Keywords: 11s gloubulin, seeds, plant protein
• Biological source: Cicer arietinum
• Total number of polymer chains: 3
• Total formula weight: 162735.36

Authors

Zhou, A.,Zhang, F. (deposition date: 2016-09-22, release date: 2017-10-04, Last modification date: 2024-11-06)

Primary citation

Sun, L.,Zhou, A.,Zhang, F.
Crystallization and crystallographic studies of a novel chickpea 11S globulin.
Acta Crystallogr.,Sect.F, 78:324-329, 2022

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: 36048082
DOI: 10.1107/S2053230X22007919

Experimental method

X-RAY DIFFRACTION (2.2 Å)