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4KFV

Structural insight into Golgi membrane stacking by GRASP65 and GRASP55

Summary for 4KFV
Entry DOI10.2210/pdb4kfv/pdb
Related4KFW
DescriptorGolgi reassembly-stacking protein 1, ZINC ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordspdz domain, golgi stacking protein, golgi, signaling protein
Biological sourceRattus norvegicus (brown rat,rat,rats)
Total number of polymer chains1
Total formula weight23151.77
Authors
Liu, X.,Hu, J. (deposition date: 2013-04-28, release date: 2013-08-21, Last modification date: 2024-03-20)
Primary citationFeng, Y.,Yu, W.,Li, X.,Lin, S.,Zhou, Y.,Hu, J.,Liu, X.
Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins
J.Biol.Chem., 288:28418-28427, 2013
Cited by
PubMed Abstract: The stacking of Golgi cisternae involves GRASP65 and GRASP55. The oligomerization of the N-terminal GRASP domain of these proteins, which consists of two tandem PDZ domains, is required to tether the Golgi membranes. However, the molecular basis for GRASP assembly is unclear. Here, we determined the crystal structures of the GRASP domain of GRASP65 and GRASP55. The structures reveal similar homotypic interactions: the GRASP domain forms a dimer in which the peptide-binding pockets of the two neighboring PDZ2 domains face each other, and the dimers are further connected by the C-terminal tail of one GRASP domain inserting into the binding pocket of the PDZ1 domain in another dimer. Biochemical analysis suggests that both types of contacts are relatively weak but are needed in combination for GRASP-mediated Golgi stacking. Our results unveil a novel mode of membrane tethering by GRASP proteins and provide insight into the mechanism of Golgi stacking.
PubMed: 23940043
DOI: 10.1074/jbc.M113.478024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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