4kfw | pdb_00004kfw

Structural insight into Golgi membrane stacking by GRASP65 and GRASP55

spinqualitylabelsall models 4kfw, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kfw is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4kfv Gene: Gorasp2, rCG_26651 (Buffalo rat) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins.,Feng Y, Yu W, Li X, Lin S, Zhou Y, Hu J, Liu X J Biol Chem. 2013 Sep 27;288(39):28418-27. doi: 10.1074/jbc.M113.478024. Epub, 2013 Aug 12. PMID:23940043 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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