Mechanism of GTPase-Activity-Induced Self-Assembly of Human Guanylate Binding Protein 1

被引：51

作者：

Voepel, Tobias ^{[1
]}

Syguda, Adrian ^{[1
]}

Britzen-Laurent, Nathalie ^{[2
]}

Kunzelmann, Simone ^{[1
]}

Luedemann, Maik-Borris ^{[1
]}

Dovengerds, Christine ^{[1
]}

Stuerzl, Michael ^{[2
]}

Herrmann, Christian ^{[1
]}

机构：

[1] Ruhr Univ Bochum, Fac Chem & Biochem, D-44780 Bochum, Germany

[2] Univ Erlangen Nurnberg, Div Mol & Expt Surg, Dept Surg, D-91054 Erlangen, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2010年 / 400卷 / 01期

关键词：

cross-linking; electrostatic interactions; GTPase; hGBP1; self-association; NUCLEOTIDE-BINDING; ENDOTHELIAL-CELLS; DOMAIN; HGBP1; VIRUS; IDENTIFICATION; INHIBITION; PHOSPHATE; GDP;

D O I：

10.1016/j.jmb.2010.04.053

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 alpha-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. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：63 / 70

页数：8

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