1DG3

STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM

Summary for 1DG3

• Entry DOI: 10.2210/pdb1dg3/pdb
• Descriptor: PROTEIN (INTERFERON-INDUCED GUANYLATE-BINDING PROTEIN 1) (2 entities in total)
• Functional Keywords: gbp, gtp hydrolysis, gdp, gmp, interferon induced, dynamin related, large gtpase family, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P32455
• Total number of polymer chains: 1
• Total formula weight: 68003.59

Authors

Prakash, B.,Praefcke, G.J.K.,Renault, L.,Wittinghofer, A.,Herrmann, C. (deposition date: 1999-11-23, release date: 2000-10-11, Last modification date: 2024-05-22)

Primary citation

Prakash, B.,Praefcke, G.J.,Renault, L.,Wittinghofer, A.,Herrmann, C.
Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins.
Nature, 403:567-571, 2000

PubMed Abstract: Interferon-gamma is an immunomodulatory substance that induces the expression of many genes to orchestrate a cellular response and establish the antiviral state of the cell. Among the most abundant antiviral proteins induced by interferon-gamma are guanylate-binding proteins such as GBP1 and GBP2. These are large GTP-binding proteins of relative molecular mass 67,000 with a high-turnover GTPase activity and an antiviral effect. Here we have determined the crystal structure of full-length human GBP1 to 1.8 A resolution. The amino-terminal 278 residues constitute a modified G domain with a number of insertions compared to the canonical Ras structure, and the carboxy-terminal part is an extended helical domain with unique features. From the structure and biochemical experiments reported here, GBP1 appears to belong to the group of large GTP-binding proteins that includes Mx and dynamin, the common property of which is the ability to undergo oligomerization with a high concentration-dependent GTPase activity.

PubMed: 10676968
DOI: 10.1038/35000617

Experimental method

X-RAY DIFFRACTION (1.8 Å)