Mechanism of GTPase-Activity-Induced Self-Assembly of Human Guanylate Binding Protein 1 |
| |
Authors: | Tobias Vöpel Adrian Syguda Nathalie Britzen-Laurent Maik-Borris Lüdemann Michael Stürzl |
| |
Institution: | 1 Physical Chemistry I, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, Universitaetsstr. 150, 44780 Bochum, Germany 2 Division of Molecular and Experimental Surgery, Department of Surgery, University of Erlangen-Nuremberg, Schwabachanlage 10, 91054 Erlangen, Germany |
| |
Abstract: | Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of large GTPases (LGs). In the course of GTP hydrolysis, the protein undergoes structural changes leading to self-assembly of the protein, which is a characteristic property of all family members. For self-assembly, the protein employs two distinct interaction sites, one of which is located within the LG domain of the protein located at the N-terminus, and the second is located in the C-terminal α-helical domain. Here, we identify intramolecular contacts between the LG domain and the helical part of hGBP1, which relay nucleotide-dependent structural changes from the N-terminus to the C-terminus and thereby mediate tetramer formation of the protein through a second contact site at the C-terminus. Furthermore, we demonstrate the impact of this intramolecular communication on the enzymatic activity of hGBP1 and on its cellular localization. |
| |
Keywords: | hGBP1 human guanylate binding protein 1 LG large GTPase wt wild type PDB Protein Data Bank DLS dynamic light scattering DTME dithio-bismaleimidoethane DTNB dithionitrobenzoic acid DMEM Dulbecco's modified Eagle's medium FBS fetal bovine serum TBS Tris-buffered saline |
本文献已被 ScienceDirect 等数据库收录! |
|