1ovn
From Proteopedia
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|PDB= 1ovn |SIZE=350|CAPTION= <scene name='initialview01'>1ovn</scene>, resolution 1.90Å | |PDB= 1ovn |SIZE=350|CAPTION= <scene name='initialview01'>1ovn</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CS:CESIUM ION'>CS</scene> | + | |LIGAND= <scene name='pdbligand=CS:CESIUM+ION'>CS</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Wind ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | |GENE= Wind ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ovn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovn OCA], [http://www.ebi.ac.uk/pdbsum/1ovn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ovn RCSB]</span> | ||
}} | }} | ||
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[[Category: Soling, H D.]] | [[Category: Soling, H D.]] | ||
[[Category: Uson, I.]] | [[Category: Uson, I.]] | ||
| - | [[Category: CS]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: dorsal-ventral patterning]] | [[Category: dorsal-ventral patterning]] | ||
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[[Category: windbeutel]] | [[Category: windbeutel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:59 2008'' |
Revision as of 19:51, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Gene: | Wind (Drosophila melanogaster) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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