Vitelline membrane outer layer protein I (VMO-I)

Function

The major role of the vitelline membrane is to prevent the mixing of the yolk and albumen and also act as an important anti-microbial barrier, as indicated by the high content of lysozyme in the outer layer Vitelline membrane outer layer protein I (VMO-I) binds tightly to ovomucin fibrils, which construct the backbone of the outer layer membrane. VMO-I has considerable activity to synthesize N-acetylchito-oligosaccharide from N-acetylglucosamine hexasaccharides but no hydrolysis activity. VMO-I is composed of 163 aa

Structure

The structure consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. Furthermore, the structure of VOMI has strong similarity to the structure of the delta-endotoxin, as well as a carbohydrate-binding site in the top region of the common fold. VMO-I revealed a unique structure of the P-prism fold, a new type of multi-sheet assembly.

References

References

1. (2005). "Exocytosis and proteomic analysis of the vesicle content of granular hemocytes from a crayfish.". Dev Comp Immunol.
2. (1995). "Characterization of vitelline membrane outer layer protein I, VMO-I: amino acid sequence and structural stability.". J Biochem.
3. (March 1994). "Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry". EMBO J..
4. (January 1996). "The beta-prism: a new folding motif". Trends Biochem. Sci..