4I6X

Crystal Structure of Non-catalyic Domain of Protein Disulfide Isomerase-related (PDIr) Protein

Summary for 4I6X

• Entry DOI: 10.2210/pdb4i6x/pdb
• Descriptor: Protein disulfide-isomerase A5 (2 entities in total)
• Functional Keywords: thioredoxin-like fold, protein binding, endoplasmic reticulum, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum lumen (By similarity): Q14554
• Total number of polymer chains: 1
• Total formula weight: 15024.34

Authors

Kozlov, G.,Vinaik, R.,Gehring, K. (deposition date: 2012-11-30, release date: 2013-04-03, Last modification date: 2024-11-06)

Primary citation

Vinaik, R.,Kozlov, G.,Gehring, K.
Structure of the Non-Catalytic Domain of the Protein Disulfide Isomerase-Related Protein (PDIR) Reveals Function in Protein Binding.
Plos One, 8:e62021-e62021, 2013

PubMed Abstract: Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as PDIA5) is a specialized member that participates in the folding of α1-antitrypsin and N-linked glycoproteins. Here, the crystal structure of the non-catalytic domain of PDIR was determined to 1.5 Å resolution. The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72. Crystal contacts between molecules potentially mimic the interactions of PDIR with misfolded substrate proteins. The results suggest that the non-catalytic domain of PDIR plays a key role in the recognition of protein partners and substrates.

PubMed: 23614004
DOI: 10.1371/journal.pone.0062021

Experimental method

X-RAY DIFFRACTION (1.5 Å)