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(New page: ==Edestin== <StructureSection load='3fz3' size='340' side='right' caption='Homolog of Edestin Protein' scene=''> == Introduction == Edestin is characterized under the Globulin family, a ...) |
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== Structural highlights == | == Structural highlights == | ||
- | Edestin is a hexamer, specific to the Cannabis sativa seed, that has a molecular mass of 300 to 400 kDa. A hexamer is a polymer molecule composed of six monomers. These subunits are identical and are arranged with 32 point group symmetry. They are related to each other by an exact 3-fold axis of symmetry and 3 dyad axes perpendicular to it. Based on this structure it can be determined that the subunit’s structure creates a large channel through the center. It has been calculated that the open ring structure has a diameter of 145 A and a depth of 90 A. The subunits, individually, contain a hydrophilic alpha-chain that is linked to a smaller hydrophobic beta-chain with a disulfide bond. When translation occurs, the alpha and beta chains polypeptides are inserted into the endoplasmic reticulum. The signal peptide is then cleaved. This cleavage creates a disulfide bridge between the chains to form a pro legumin, a protein precursor. Next, three subunits link together to form a trimer in the endoplasmic reticulum and then transported to the vacuole. In the vacuole, the cleavage of the chains within the trimers signals protein maturation. Protein maturation connects two trimers together to form the hexameric protein. The trimers that form the center of the hexameric protein are beta-sheet barrels. The trimers that form the outer region of the hexameric protein consist of alpha-helices. A calcium ion ligand can be found adjacent to the Leucine 330 E residue. The calcium ion ligand is residue CA 10 CA. The ligand interaction with the edestin protein has yet to be specified. | + | Edestin is a hexamer, specific to the Cannabis sativa seed, that has a molecular mass of 300 to 400 kDa. A hexamer is a polymer molecule composed of six monomers. These subunits are identical and are arranged with 32 point group symmetry. They are related to each other by an exact 3-fold axis of symmetry and 3 dyad axes perpendicular to it. Based on this structure it can be determined that the subunit’s structure creates a large channel through the center. It has been calculated that the <scene name='91/911199/Open_ring_structure/1'>open ring structure</scene> has a diameter of 145 A and a depth of 90 A. The subunits, individually, contain a <scene name='91/911199/Alpha_chain/1'>hydrophilic alpha-chain</scene> that is linked to a smaller <scene name='91/911199/Beta_chain/1'>hydrophobic beta-chain</scene> with a disulfide bond. When translation occurs, the alpha and beta chains polypeptides are inserted into the endoplasmic reticulum. The signal peptide is then cleaved. This cleavage creates a disulfide bridge between the chains to form a pro legumin, a protein precursor. Next, three subunits link together to form a trimer in the endoplasmic reticulum and then transported to the vacuole. In the vacuole, the cleavage of the chains within the trimers signals protein maturation. Protein maturation connects two trimers together to form the hexameric protein. The trimers that form the center of the hexameric protein are beta-sheet barrels. The trimers that form the outer region of the hexameric protein consist of alpha-helices. A calcium ion ligand can be found adjacent to the Leucine 330 E residue. The <scene name='91/911199/Calcium_ion/1'>calcium ion ligand</scene> is residue CA 10 CA. The ligand interaction with the edestin protein has yet to be specified. |
The reference protein used is almond Pru1 protein. This protein is a homologous structure to the Edestin protein. Pru1 protein is a seed storage protein that creates required nutrition for seed germination and sprout growth. The difference between these two proteins is the Pru1 protein has been identified as an allergenic protein and Edestin has not. The structure of the Pru1 protein is similar to the Edestin protein because of the hexameric shape. Pru1 protein is a combination of two trimers while Edestin was found to be the formation of 3 trimers. The Pru1 protein also contains Calcium and Sodium Ion ligands. The Edestin protein only contains a Calcium ion ligand. <ref name="Pru1">doi:10.1021/jf9017355</ref> | The reference protein used is almond Pru1 protein. This protein is a homologous structure to the Edestin protein. Pru1 protein is a seed storage protein that creates required nutrition for seed germination and sprout growth. The difference between these two proteins is the Pru1 protein has been identified as an allergenic protein and Edestin has not. The structure of the Pru1 protein is similar to the Edestin protein because of the hexameric shape. Pru1 protein is a combination of two trimers while Edestin was found to be the formation of 3 trimers. The Pru1 protein also contains Calcium and Sodium Ion ligands. The Edestin protein only contains a Calcium ion ligand. <ref name="Pru1">doi:10.1021/jf9017355</ref> |
Revision as of 19:09, 28 April 2022
Edestin
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References
- ↑ Docimo T, Caruso I, Ponzoni E, Mattana M, Galasso I. Molecular characterization of edestin gene family in Cannabis sativa L. Plant Physiol Biochem. 2014 Nov;84:142-148. doi: 10.1016/j.plaphy.2014.09.011., Epub 2014 Sep 24. PMID:25280223 doi:http://dx.doi.org/10.1016/j.plaphy.2014.09.011
- ↑ Tang CH, Ten Z, Wang XS, Yang XQ. Physicochemical and functional properties of hemp (Cannabis sativa L.) protein isolate. J Agric Food Chem. 2006 Nov 15;54(23):8945-50. doi: 10.1021/jf0619176. PMID:17090145 doi:http://dx.doi.org/10.1021/jf0619176
- ↑ Malomo SA, He R, Aluko RE. Structural and functional properties of hemp seed protein products. J Food Sci. 2014 Aug;79(8):C1512-21. doi: 10.1111/1750-3841.12537. Epub 2014 Jul , 21. PMID:25048774 doi:http://dx.doi.org/10.1111/1750-3841.12537
- ↑ Jin T, Albillos SM, Guo F, Howard A, Fu TJ, Kothary MH, Zhang YZ. Crystal structure of prunin-1, a major component of the almond (Prunus dulcis) allergen amandin. J Agric Food Chem. 2009 Sep 23;57(18):8643-51. PMID:19694440 doi:10.1021/jf9017355