1HCE

STRUCTURE OF HISACTOPHILIN IS SIMILAR TO INTERLEUKIN-1 BETA AND FIBROBLAST GROWTH FACTOR

Summary for 1HCE

• Entry DOI: 10.2210/pdb1hce/pdb
• Descriptor: HISACTOPHILIN (1 entity in total)
• Functional Keywords: actin binding
• Biological source: Dictyostelium discoideum
• Cellular location: Cytoplasm: P13231
• Total number of polymer chains: 1
• Total formula weight: 13496.91

Authors

Habazettl, J.,Gondol, D.,Wiltscheck, R.,Otlewski, J.,Schleicher, M.,Holak, T.A. (deposition date: 1994-07-12, release date: 1994-09-30, Last modification date: 2024-05-01)

Primary citation

Habazettl, J.,Gondol, D.,Wiltscheck, R.,Otlewski, J.,Schleicher, M.,Holak, T.A.
Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.
Nature, 359:855-858, 1992

PubMed Abstract: The fast reaction of the actin-based cytoskeleton in motile cells after stimulation with a chemoattractant requires a signal-transduction chain that creates a very specific environment at distinct regions beneath the plasma membrane. Dictyostelium hisactophilin, a unique actin-binding protein, is a submembranous pH sensor that signals slight changes of the H+ concentration to actin by inducing actin polymerization and binding to microfilaments only at pH values below seven. It has a relative molecular mass of 13.5K and its most unusual feature is the presence of 31 histidine residues among its total of 118 amino acids. The transduction of an external signal from the plasma membrane to the cytoskeleton is poorly understood. Here we report the protein's structure in solution determined by nuclear magnetic resonance spectroscopy. The nuclear Overhauser effect intensities of the three-dimensional nuclear Overhauser spectra were used directly in the calculations. The overall folding of histactophilin is similar to that of interleukin-1 beta and fibroblast growth factor, but the primary amino-acid sequence of hisactophilin is unrelated to these two proteins.

PubMed: 1436061
DOI: 10.1038/359855a0

Experimental method

SOLUTION NMR