Last updated Phosvitin structure adapted from vitellogenin AlphaFold (AF-P02845-F1; residues 1112-1328) with serine residues highlighted in red. Visualized using ChimeraX.
Phosvitin is one of the egg (commonly hen's egg) yolk[1][2]phosphoproteins known for being the most phosphorylatedprotein found in nature.[3][4][5] Phosvitin isolation was first described by Mecham and Olcott in the year 1949.[3][6] Recently[when?] it has been shown that phosvitin orchestrates nucleation and growth of biomimetic bone like apatite.[7]
As the most phosphorylated natural protein, phosvitin contains 123 phosphoserine residues accounting for 56.7% of its total 217 amino acid residues.[3][8] The structure of phosvitin at large consists of 4-12 base pair stretches of serines, interspersed with amino acid residues lysine (6.9%), histidine (6.0%), and arginine (5.1%), among others in smaller quantities.[9] Phosvitin’s structure (right) is adapted from the protein vitellogenin (Gene: VTG2; Uniprot: P02845; residues 1-1850) generated by AlphaFold, where all the possible phosphorylated serine residues are highlighted in red. Phosvitin is one of four proteins cleaved from vitellogenin and is unstructured at neutral pH.[3] Despite phosvitin only accounting for 16% of total proteins in egg yolk, it alone accounts for 60% of the total yolk phosphoproteins as well as 90% of the total yolk phosphorus.[10][8]
Function
Due to phosvitin’s polyanionic activity, the protein performs functionalities such as metal chelation, emulsification, and nutrition sequestration for a growing embryo.[3] Additionally, in recent[when?] research it has been shown that the disordered secondary structure of phosvitin orchestrates nucleation and growth of biomimetic bone like apatite.[7]
References
↑ Joubert, F. J.; Cook, W. H. (1958). "Preparation And Characterization Of Phosvitin From Hen Egg Yolk". Canadian Journal of Biochemistry and Physiology. 36 (4): 399–408. doi:10.1139/o58-045. PMID13511246.
↑ Clark, Richard C. (1980). "Relative and total abundance of constituent phosphoproteins from hen phosvitin in egg yolk". International Journal of Biochemistry. 12 (4): 651–653. doi:10.1016/0020-711x(80)90021-x. PMID7428998.
↑ Taborsky, George (1963). "Interaction Between Phosvitin and Iron and Its Effect on a Rearrangement of Phosvitin Structure". Biochemistry. 2 (2): 266–271. doi:10.1021/bi00902a010. PMID13980103.
↑ Jung, Samooel; etal. (Dec 2012). "The functional property of egg yolk phosvitin as a melanogenesis inhibitor". Food Chemistry. 135 (3): 993–998. doi:10.1016/j.foodchem.2012.05.113. PMID22953815.
SI, Ishikawa; etal. (Aug 2007). "Egg yolk protein and egg yolk phosvitin inhibit calcium, magnesium, and iron absorptions in rats". Journal of Food Science. 72 (6): S412 –S419. doi:10.1111/j.1750-3841.2007.00417.x. PMID17995699.
Mecham, Dale K.; Olcott, Harold S. (1949). "Phosvitin, the principal phosphoprotein of egg yolk". Journal of the American Chemical Society. 71 (11): 3670–3679. Bibcode:1949JAChS..71.3670M. doi:10.1021/ja01179a028.
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