1OVN

Crystal Structure and Functional Analysis of Drosophila Wind-- a PDI-Related Protein

Summary for 1OVN

• Entry DOI: 10.2210/pdb1ovn/pdb
• Descriptor: Windbeutel, CESIUM ION (3 entities in total)
• Functional Keywords: wind, windbeutel, pdi-dbeta, pdi, protein disulfide isomerase, pipe, dorsal-ventral patterning, chaperone
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Endoplasmic reticulum lumen : O44342
• Total number of polymer chains: 2
• Total formula weight: 57227.95

Authors

Ma, Q.,Guo, C.,Barnewitz, K.,Sheldrick, G.M.,Soling, H.D.,Uson, I.,Ferrari, D.M. (deposition date: 2003-03-27, release date: 2004-02-24, Last modification date: 2024-11-20)

Primary citation

Ma, Q.,Guo, C.,Barnewitz, K.,Sheldrick, G.M.,Soling, H.D.,Uson, I.,Ferrari, D.M.
Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein.
J.Biol.Chem., 278:44600-44607, 2003

PubMed Abstract: 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.

PubMed: 12941941
DOI: 10.1074/jbc.M307966200

Experimental method

X-RAY DIFFRACTION (1.9 Å)