2QC7: Crystal Structure Of The Protein-disulfide Isomerase Related Chaperone Erp29

The protein disulfide isomerase-related protein ERp29 is a putative chaperone involved in processing and secretion of secretory proteins. Until now, however, both the structure and the exact nature of interacting substrates remained unclear. We provide for the first time a crystal structure of human ERp29, refined to 2.9 A, and show that the protein has considerable structural homology to its Drosophila homolog Wind. We show that ERp29 binds directly not only to thyroglobulin and thyroglobulin-derived peptides in vitro but also to the Wind client protein Pipe and Pipe-derived peptides, although it fails to process Pipe in vivo. A monomeric mutant of ERp29 and a D domain mutant in which the second peptide binding site is inactivated also bind protein substrates, indicating that the monomeric thioredoxin domain is sufficient for client protein binding. Indeed, the b domains of ERp29 or Wind, expressed alone, are sufficient for binding proteins and peptides. Interacting peptides have in common two or more aromatic residues, with stronger binding for sequences with overall basic character. Thus, the data allow a view of the two putative peptide binding sites of ERp29 and indicate that the apparent, different processing activity of the human and Drosophila proteins in vivo does not stem from differences in peptide binding properties.
PDB ID: 2QC7Download
MMDB ID: 65034
PDB Deposition Date: 2007/6/19
Updated in MMDB: 2009/07
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 2QC7: dimeric; determined by author
Molecular Components in 2QC7
Label Count Molecule
Proteins (2 molecules)
Endoplasmic Reticulum Protein Erp29(Gene symbol: ERP29)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB