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http://purl.uniprot.org/citations/8131734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8131734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8131734http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of vitelline membrane outer layer protein I (VMO-I), which is isolated from the vitelline membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06348.x"xsd:string
http://purl.uniprot.org/citations/8131734http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06348.x"xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Morikawa K."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Morikawa K."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Shimizu T."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Shimizu T."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Vassylyev D.G."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Vassylyev D.G."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Doi Y."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Doi Y."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Kido S."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/author"Kido S."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/pages"1003-1010"xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/pages"1003-1010"xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/title"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."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/title"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."xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8131734http://purl.uniprot.org/core/volume"13"xsd:string