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1R1Z

The Crystal structure of the Carbohydrate recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals a novel metal binding site and conformational changes associated with calcium ion binding

Summary for 1R1Z
Entry DOI10.2210/pdb1r1z/pdb
Related1gv9
DescriptorERGIC-53 protein, CALCIUM ION (3 entities in total)
Functional Keywordsbeta-sheet, calcium-binding, lectin, mammalian, endoplasmic reticulum, sugar binding protein
Biological sourceRattus norvegicus (Norway rat)
Cellular locationEndoplasmic reticulum-Golgi intermediate compartment membrane; Single-pass type I membrane protein (By similarity): Q62902
Total number of polymer chains4
Total formula weight116429.57
Authors
Velloso, L.M.,Svensson, K.,Pettersson, R.F.,Lindqvist, Y. (deposition date: 2003-09-25, release date: 2003-12-16, Last modification date: 2024-10-30)
Primary citationVelloso, L.M.,Svensson, K.,Pettersson, R.F.,Lindqvist, Y.
The Crystal Structure of the Carbohydrate-recognition Domain of the Glycoprotein Sorting Receptor p58/ERGIC-53 Reveals an Unpredicted Metal-binding Site and Conformational Changes Associated with Calcium Ion Binding.
J.Mol.Biol., 334:845-851, 2003
Cited by
PubMed Abstract: p58/ERGIC-53 is a calcium-dependent animal lectin that acts as a cargo receptor, binding to a set of glycoproteins in the endoplasmic reticulum (ER) and transporting them to the Golgi complex. It is similar in structure to calcium-dependent leguminous lectins. We have determined the structure of the carbohydrate-recognition domain of p58/ERGIC-53 in its calcium-bound form. The structure reveals localized but large conformational changes in relation to the previously determined metal ion-free structure, mapping mostly to the ligand-binding site. It reveals the presence of two calcium ion-binding sites located 6A apart, one of which has no equivalent in the plant lectins. The second metal ion-binding site present in that class of lectins, binding Mn(2+), is absent from p58/ERGIC-53. The absence of a short loop in the ligand-binding site in this protein suggests that it has adapted to optimally bind the high-mannose Man(8)(GlcNAc)(2) glycan common to glycoproteins at the ER exit stage.
PubMed: 14643651
DOI: 10.1016/j.jmb.2003.10.031
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2025-06-18公开中

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