4REY

Crystal Structure of the GRASP65-GM130 C-terminal peptide complex

Summary for 4REY

• Entry DOI: 10.2210/pdb4rey/pdb
• Descriptor: Golgi reassembly-stacking protein 1, Golgin subfamily A member 2, SULFATE ION, ... (4 entities in total)
• Functional Keywords: pdz fold six-stranded anti parallel-barrel capped by two-helices, protein interaction, membrane protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, cis-Golgi network membrane ; Peripheral membrane protein ; Cytoplasmic side : Q9BQQ3; Golgi apparatus, cis-Golgi network membrane ; Peripheral membrane protein : Q08379
• Total number of polymer chains: 2
• Total formula weight: 26422.63

Authors

Shi, N.,Hu, F.,Li, B. (deposition date: 2014-09-24, release date: 2015-09-23, Last modification date: 2023-09-20)

Primary citation

Hu, F.,Shi, X.,Li, B.,Huang, X.,Morelli, X.,Shi, N.
Structural Basis for the Interaction between the Golgi Reassembly-stacking Protein GRASP65 and the Golgi Matrix Protein GM130.
J.Biol.Chem., 290:26373-26382, 2015

PubMed Abstract: GM130 and GRASP65 are Golgi peripheral membrane proteins that play a key role in Golgi stacking and vesicle tethering. However, the molecular details of their interaction and their structural role as a functional unit remain unclear. Here, we present the crystal structure of the PDZ domains of GRASP65 in complex with the GM130 C-terminal peptide at 1.96-Å resolution. In contrast to previous findings proposing that GM130 interacts with GRASP65 at the PDZ2 domain only, our crystal structure of the complex indicates that GM130 binds to GRASP65 at two distinct sites concurrently and that both the PDZ1 and PDZ2 domains of GRASP65 participate in this molecular interaction. Mutagenesis experiments support these structural observations and demonstrate that they are required for GRASP65-GM130 association.

PubMed: 26363069
DOI: 10.1074/jbc.M115.657940

Experimental method

X-RAY DIFFRACTION (1.96 Å)