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1G8I

CRYSTAL STRUCTURE OF HUMAN FREQUENIN (NEURONAL CALCIUM SENSOR 1)

Summary for 1G8I
Entry DOI10.2210/pdb1g8i/pdb
Related1BJF 1REC
DescriptorNEURONAL CALCIUM SENSOR 1, SODIUM ION, CALCIUM ION, ... (7 entities in total)
Functional Keywordscalcium binding-protein, ef-hand, calcium ion, metal binding protein
Biological sourceHomo sapiens (human)
Cellular locationGolgi apparatus, Golgi stack membrane; Peripheral membrane protein: P62166
Total number of polymer chains2
Total formula weight45213.09
Authors
Bourne, Y.,Dannenberg, J.,Pollmann, V.,Marchot, P.,Pongs, O. (deposition date: 2000-11-17, release date: 2001-05-09, Last modification date: 2023-08-09)
Primary citationBourne, Y.,Dannenberg, J.,Pollmann, V.,Marchot, P.,Pongs, O.
Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1).
J.Biol.Chem., 276:11949-11955, 2001
Cited by
PubMed Abstract: Frequenin, a member of a large family of myristoyl-switch calcium-binding proteins, functions as a calcium-ion sensor to modulate synaptic activity and secretion. We show that human frequenin colocalizes with ARF1 GTPase in COS-7 cells and occurs in similar cellular compartments as the phosphatidylinositol-4-OH kinase PI4Kbeta, the mammalian homolog of the yeast kinase PIK1. In addition, the crystal structure of unmyristoylated, calcium-bound human frequenin has been determined and refined to 1.9 A resolution. The overall fold of frequenin resembles those of neurocalcin and the photoreceptor, recoverin, of the same family, with two pairs of calcium-binding EF hands and three bound calcium ions. Despite the similarities, however, frequenin displays significant structural differences. A large conformational shift of the C-terminal region creates a wide hydrophobic crevice at the surface of frequenin. This crevice, which is unique to frequenin and distinct from the myristoyl-binding box of recoverin, may accommodate a yet unknown protein ligand.
PubMed: 11092894
DOI: 10.1074/jbc.M009373200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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