1r1z
From Proteopedia
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|PDB= 1r1z |SIZE=350|CAPTION= <scene name='initialview01'>1r1z</scene>, resolution 2.40Å | |PDB= 1r1z |SIZE=350|CAPTION= <scene name='initialview01'>1r1z</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= LMAN1 OR ERGIC53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= LMAN1 OR ERGIC53 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1gv9|1GV9]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1z OCA], [http://www.ebi.ac.uk/pdbsum/1r1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r1z RCSB]</span> | ||
}} | }} | ||
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[[Category: Svensson, K.]] | [[Category: Svensson, K.]] | ||
[[Category: Velloso, L M.]] | [[Category: Velloso, L M.]] | ||
- | [[Category: CA]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
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[[Category: mammalian]] | [[Category: mammalian]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:07 2008'' |
Revision as of 20:22, 30 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | |||||||
Gene: | LMAN1 OR ERGIC53 (Rattus norvegicus) | ||||||
Related: | 1GV9
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
Overview
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.
About this Structure
1R1Z is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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., Velloso LM, Svensson K, Pettersson RF, Lindqvist Y, J Mol Biol. 2003 Dec 12;334(5):845-51. PMID:14643651
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