Summary: Vitelline membrane outer layer protein I (VOMI)
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Vitelline membrane outer layer protein I (VMO-I) Edit Wikipedia article
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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
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
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.
- 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. 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. 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.
Vitelline membrane outer layer protein I (VOMI) Provide feedback
VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure  that 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 .
Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K; , EMBO J 1994;13:1003-1010.: 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. PUBMED:8131734 EPMC:8131734
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005515
VOMI binds tightly to ovomucin fibrils of the egg yolk membrane. The structure [PUBMED:8131734] 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 [PUBMED:8848836].
|Biological process||vitelline membrane formation (GO:0030704)|
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Curation and family details
|Seed source:||Pfam-B_3481 (release 7.0)|
|Number in seed:||22|
|Number in full:||120|
|Average length of the domain:||149.20 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||64.05 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the VOMI domain has been found. There are 2 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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