4r0y

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

spinqualitylabelsall models 4r0y, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r0y is a 2 chain structure with sequence from Escherichia coli K-12 and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.DLGP1_RAT Part of the postsynaptic scaffold in neuronal cells. Publication Abstract from PubMed 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 2.0A resolution. The structure of GKAP GH1 displays a three-helix bundle connected by short flexible loops. The predicted helix alpha4 which was not visible in the crystal structure associates weakly with the helix alpha3 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. Structure of the GH1 domain of guanylate kinase-associated protein from Rattus norvegicus.,Tong J, Yang H, Eom SH, Chun C, Im YJ Biochem Biophys Res Commun. 2014 Aug 22. pii: S0006-291X(14)01496-X. doi:, 10.1016/j.bbrc.2014.08.073. PMID:25152391 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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