1vmo
From Proteopedia
(New page: 200px<br /><applet load="1vmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vmo, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1vmo.gif|left|200px]]<br /><applet load="1vmo" size=" | + | [[Image:1vmo.gif|left|200px]]<br /><applet load="1vmo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vmo, resolution 2.2Å" /> | caption="1vmo, resolution 2.2Å" /> | ||
'''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 /> | '''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== | ==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 | + | 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== | ==About this Structure== | ||
| - | 1VMO 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:// | + | 1VMO 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== | ==Reference== | ||
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[[Category: Morikawa, K.]] | [[Category: Morikawa, K.]] | ||
[[Category: Shimizu, T.]] | [[Category: Shimizu, T.]] | ||
| - | [[Category: Vassylyev, D | + | [[Category: Vassylyev, D G.]] |
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:51 2008'' |
Revision as of 13:36, 21 February 2008
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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
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