Vitelline membrane outer layer protein I (VMO-I)
| VOMI | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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 | |||||||||
| Identifiers | |||||||||
| Symbol | VOMI | ||||||||
| Pfam | PF03762 | ||||||||
| InterPro | IPR005515 | ||||||||
| SCOP2 | 1vmo / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, this entry refers to a protein domain called, the Vitelline membrane outer layer protein I (VMO-I). It is a structure found on the outside of an egg, in the vitelline membrane.
Function[edit]
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 [1] 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[2]
Structure[edit]
The structure[3] 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.[4] VMO-I revealed a unique structure of the P-prism fold, a new type of multi-sheet assembly.
References[edit]
- ^ Sricharoen S, Kim JJ, Tunkijjanukij S, Söderhäll I (2005). "Exocytosis and proteomic analysis of the vesicle content of granular hemocytes from a crayfish". Dev Comp Immunol. 29 (12): 1017–31. doi:10.1016/j.dci.2005.03.010. PMID 15975654.
- ^ Kido S, Doi Y, Kim F, Morishita E, Narita H, Kanaya S, et al. (1995). "Characterization of vitelline membrane outer layer protein I, VMO-I: amino acid sequence and structural stability". J Biochem. 117 (6): 1183–91. doi:10.1093/oxfordjournals.jbchem.a124842. PMID 7490258.
- ^ Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K (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. 13 (5): 1003–10. doi:10.1002/j.1460-2075.1994.tb06348.x. PMC 394907. PMID 8131734.
- ^ Shimizu T, Morikawa K (January 1996). "The beta-prism: a new folding motif". Trends Biochem. Sci. 21 (1): 3–6. doi:10.1016/s0968-0004(06)80018-6. PMID 8848836.