1vmo: Difference between revisions

Revision as of 16:36, 21 February 2008

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

OverviewOverview

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 StructureAbout this Structure

1VMO is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 15:36:51 2008

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OCA

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-[[Image:1vmo.gif|left|200px]]<br /><applet load="1vmo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1vmo.gif|left|200px]]<br /><applet load="1vmo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1vmo, resolution 2.2&Aring;" />
 '''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'''<br />
 ==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.
+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==
-VMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VMO OCA].
+VMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VMO OCA].
 ==Reference==
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 [[Category: Morikawa, K.]]
 [[Category: Shimizu, T.]]
-[[Category: Vassylyev, D.G.]]
+[[Category: Vassylyev, D G.]]
 [[Category: membrane protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:57:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:51 2008''