1GV9

p58/ERGIC-53

Summary for 1GV9

• Entry DOI: 10.2210/pdb1gv9/pdb
• Descriptor: P58/ERGIC-53, SULFATE ION (3 entities in total)
• Functional Keywords: lectin, carbohydrate binding
• Biological source: RATTUS NORVEGICUS (RAT)
• Cellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane ; Single-pass type I membrane protein : Q62902
• Total number of polymer chains: 1
• Total formula weight: 28493.45

Authors

Velloso, L.M.,Svensson, K.,Schneider, G.,Pettersson, R.F.,Lindqvist, Y. (deposition date: 2002-02-07, release date: 2002-02-28, Last modification date: 2024-10-23)

Primary citation

Velloso, L.M.,Svensson, K.,Schneider, G.,Pettersson, R.F.,Lindqvist, Y.
Crystal Structure of the Carbohydrate Recognition Domain of P58/Ergic-53, a Protein Involved in Glycoprotein Export from the Endoplasmic Reticulum.
J.Biol.Chem., 277:15979-, 2002

PubMed Abstract: p58/ERGIC-53 is an animal calcium-dependent lectin that cycles between the endoplasmic reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of soluble glycoproteins exported from the ER. We have determined the crystal structure of the carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to 1.46 A resolution. The fold and ligand binding site are most similar to those of leguminous lectins. The structure also resembles that of the CRD of the ER folding chaperone calnexin and the neurexins, a family of non-lectin proteins expressed on neurons. The CRD comprises one concave and one convex beta-sheet packed into a beta-sandwich. The ligand binding site resides in a negatively charged cleft formed by conserved residues. A large surface patch of conserved residues with a putative role in protein-protein interactions and oligomerization lies on the opposite side of the ligand binding site. Together with previous functional data, the structure defines a new and expanding class of calcium-dependent animal lectins and provides a starting point for the understanding of glycoprotein sorting between the ER and the Golgi.

PubMed: 11850423
DOI: 10.1074/JBC.M112098200

Experimental method

X-RAY DIFFRACTION (1.46 Å)