2QC7

Crystal structure of the protein-disulfide isomerase related chaperone ERp29

Summary for 2QC7

• Entry DOI: 10.2210/pdb2qc7/pdb
• Related: 1G7D 1G7E 1OVN
• Descriptor: Endoplasmic reticulum protein ERp29 (1 entity in total)
• Functional Keywords: b domain (residues 33-153), d domain (residues 154-261), chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum lumen: P30040
• Total number of polymer chains: 2
• Total formula weight: 54444.12

Authors

Barak, N.N.,Sevvana, M.,Neumann, P.,Malesevic, M.,Naumann, K.,Fischer, G.,Sheldrick, G.M.,Stubbs, M.T.,Ferrari, D.M. (deposition date: 2007-06-19, release date: 2008-06-24, Last modification date: 2023-08-30)

Primary citation

Barak, N.N.,Neumann, P.,Sevvana, M.,Schutkowski, M.,Naumann, K.,Malesevic, M.,Reichardt, H.,Fischer, G.,Stubbs, M.T.,Ferrari, D.M.
Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29.
J.Mol.Biol., 385:1630-1642, 2009

PubMed Abstract: 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.

PubMed: 19084538
DOI: 10.1016/j.jmb.2008.11.052

Experimental method

X-RAY DIFFRACTION (2.9 Å)