1VMO

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

Summary for 1VMO

• Entry DOI: 10.2210/pdb1vmo/pdb
• Descriptor: VITELLINE MEMBRANE OUTER LAYER PROTEIN I (2 entities in total)
• Functional Keywords: membrane protein
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P41366
• Total number of polymer chains: 2
• Total formula weight: 36000.61

Authors

Shimizu, T.,Vassylyev, D.G.,Kido, S.,Doi, Y.,Morikawa, K. (deposition date: 1994-01-06, release date: 1994-05-31, Last modification date: 2024-10-30)

Primary citation

Shimizu, T.,Vassylyev, D.G.,Kido, S.,Doi, Y.,Morikawa, K.
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., 13:1003-1010, 1994

PubMed Abstract: 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.

PubMed: 8131734

Experimental method

X-RAY DIFFRACTION (2.2 Å)