1ovn

From Proteopedia

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 CS 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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