5gyl

Structure of Cicer arietinum 11S gloubulin

spinqualitylabelsall models 5gyl, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gyl is a 3 chain structure with sequence from Cicer arietinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA