4R0Y

Structure of Maltose-binding Protein Fusion with the C-terminal GH1 domain of Guanylate Kinase-associated Protein from Rattus norvegicus

Summary for 4R0Y

• Entry DOI: 10.2210/pdb4r0y/pdb
• Descriptor: Maltose-binding periplasmic protein, Disks large-associated protein 1 (2 entities in total)
• Functional Keywords: three-helix bundle, synaptic scaffolding protein, protein binding
• Biological source: Escherichia coli K-12 (rat); More
• Cellular location: Cell membrane; Peripheral membrane protein: P97836
• Total number of polymer chains: 2
• Total formula weight: 112435.45

Authors

Im, Y.J.,Tong, J. (deposition date: 2014-08-03, release date: 2014-09-10, Last modification date: 2023-11-08)

Primary citation

Tong, J.,Yang, H.,Eom, S.H.,Chun, C.,Im, Y.J.
Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus.
Biochem.Biophys.Res.Commun., 452:130-135, 2014

PubMed Abstract: Guanylate-kinase-associated protein (GKAP) is a scaffolding protein that links NMDA receptor-PSD-95 to Shank-Homer complexes by protein-protein interactions at the synaptic junction. GKAP family proteins are characterized by the presence of a C-terminal conserved GKAP homology domain 1 (GH1) of unknown structure and function. In this study, crystal structure of the GH1 domain of GKAP from Rattus norvegicus was determined in fusion with an N-terminal maltose-binding protein at 2.0 Å resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix α4 which was not visible in the crystal structure associates weakly with the helix α3 suggesting dynamic nature of the GH1 domain. The strict conservation of GH1 domain across GKAP family members and the lack of a catalytic active site required for enzyme activity imply that the GH1 domain might serve as a protein-protein interaction module for the synaptic protein clustering.

PubMed: 25152391
DOI: 10.1016/j.bbrc.2014.08.073

Experimental method

X-RAY DIFFRACTION (2 Å)