1vmo
From Proteopedia
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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
Overview
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.
About this Structure
1VMO is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
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. 1994 Mar 1;13(5):1003-10. PMID:8131734
Page seeded by OCA on Wed Nov 21 04:57:35 2007
