IPR005515
Vitelline membrane outer layer protein I (VOMI)
InterPro entry
Short name | VOMI |
Overlapping homologous superfamilies |
Description
Vitelline membrane outer layer protein I (VMO-I) is one of the proteins found in the outer layer of the vitelline membrane of eggs. VMO-I, lysozyme, and VMO-II are bound tightly to ovomucin fibrils of the egg yolk membrane. The structure of VMO-I
[1] consists of three β-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. It is a member of the β-prism-fold family and the structure of VOM-I 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
[2]. VMO-I has been shown to synthesize N-acetylchito-oligosaccharides from N-acetylglucosamine.
References
1.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. Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K. EMBO J. 13, 1003-10, (1994). View articlePMID: 8131734
2.The beta-prism: a new folding motif. Shimizu T, Morikawa K. Trends Biochem. Sci. 21, 3-6, (1996). View articlePMID: 8848836