1ovn
From Proteopedia
(New page: 200px<br /><applet load="1ovn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ovn, resolution 1.90Å" /> '''Crystal Structure an...) |
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| - | [[Image:1ovn.jpg|left|200px]]<br /><applet load="1ovn" size=" | + | [[Image:1ovn.jpg|left|200px]]<br /><applet load="1ovn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ovn, resolution 1.90Å" /> | caption="1ovn, resolution 1.90Å" /> | ||
'''Crystal Structure and Functional Analysis of Drosophila Wind-- a PDI-Related Protein'''<br /> | '''Crystal Structure and Functional Analysis of Drosophila Wind-- a PDI-Related Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the developing Drosophila melanogaster embryo, dorsal-ventral | + | In the developing Drosophila melanogaster embryo, dorsal-ventral patterning displays an absolute requirement for the product of the essential windbeutel gene, Wind. In homozygous windbeutel mutant flies, dorsal-ventral patterning fails to initiate because of the failure of the Golgi-resident proteoglycan-modifying protein, Pipe, to exit the endoplasmic reticulum, and this leads to the death of the embryo. Here, we describe the three-dimensional structure of Wind at 1.9-A resolution and identify a candidate surface for interaction with Pipe. This represents the first crystal structure of a eukaryotic protein-disulfide isomerase-related protein of the endoplasmic reticulum to be described. The dimeric protein is composed of an N-terminal thioredoxin domain and a C-terminal alpha-helical domain unique to protein-disulfide isomerase D proteins. Although Wind carries a CXXC motif that is partially surface accessible, this motif is redox inactive, and the cysteines are not required for the targeting of Pipe to the Golgi. However, both domains are required for targeting Pipe to the Golgi, and, although the mouse homologue ERp28 cannot replace the function of Wind, exchange of the Wind D-domain with that of ERp28 allows for efficient Golgi transport of Pipe. |
==About this Structure== | ==About this Structure== | ||
| - | 1OVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with CS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1OVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=CS:'>CS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barnewitz, K.]] | [[Category: Barnewitz, K.]] | ||
| - | [[Category: Ferrari, D | + | [[Category: Ferrari, D M.]] |
[[Category: Guo, C.]] | [[Category: Guo, C.]] | ||
[[Category: Ma, Q.]] | [[Category: Ma, Q.]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
| - | [[Category: Soling, H | + | [[Category: Soling, H D.]] |
[[Category: Uson, I.]] | [[Category: Uson, I.]] | ||
[[Category: CS]] | [[Category: CS]] | ||
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[[Category: windbeutel]] | [[Category: windbeutel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:06 2008'' |
Revision as of 12:22, 21 February 2008
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Crystal Structure and Functional Analysis of Drosophila Wind-- a PDI-Related Protein
Overview
In the developing Drosophila melanogaster embryo, dorsal-ventral patterning displays an absolute requirement for the product of the essential windbeutel gene, Wind. In homozygous windbeutel mutant flies, dorsal-ventral patterning fails to initiate because of the failure of the Golgi-resident proteoglycan-modifying protein, Pipe, to exit the endoplasmic reticulum, and this leads to the death of the embryo. Here, we describe the three-dimensional structure of Wind at 1.9-A resolution and identify a candidate surface for interaction with Pipe. This represents the first crystal structure of a eukaryotic protein-disulfide isomerase-related protein of the endoplasmic reticulum to be described. The dimeric protein is composed of an N-terminal thioredoxin domain and a C-terminal alpha-helical domain unique to protein-disulfide isomerase D proteins. Although Wind carries a CXXC motif that is partially surface accessible, this motif is redox inactive, and the cysteines are not required for the targeting of Pipe to the Golgi. However, both domains are required for targeting Pipe to the Golgi, and, although the mouse homologue ERp28 cannot replace the function of Wind, exchange of the Wind D-domain with that of ERp28 allows for efficient Golgi transport of Pipe.
About this Structure
1OVN is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein., Ma Q, Guo C, Barnewitz K, Sheldrick GM, Soling HD, Uson I, Ferrari DM, J Biol Chem. 2003 Nov 7;278(45):44600-7. Epub 2003 Aug 26. PMID:12941941
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