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Mechanism of GTPase-activity-induced self-assembly of human guanylate binding protein 1.

Voepel T, Syguda A, Britzen-Laurent N, Kunzelmann S, Luedemann MB, Dovengerds C, Stürzl M, Herrmann C (2010)

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Publication Status: Published

Publication Type: Journal article

Publication year: 2010

Journal

Book Volume: 400

Pages Range: 63-70

Journal Issue: 1

DOI: 10.1016/j.jmb.2010.04.053

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 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.

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APA:

Voepel, T., Syguda, A., Britzen-Laurent, N., Kunzelmann, S., Luedemann, M.-B., Dovengerds, C.,... Herrmann, C. (2010). Mechanism of GTPase-activity-induced self-assembly of human guanylate binding protein 1. Journal of Molecular Biology, 400(1), 63-70. https://doi.org/10.1016/j.jmb.2010.04.053

MLA:

Voepel, Tobias, et al. "Mechanism of GTPase-activity-induced self-assembly of human guanylate binding protein 1." Journal of Molecular Biology 400.1 (2010): 63-70.

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