1F5N

HUMAN GUANYLATE BINDING PROTEIN-1 IN COMPLEX WITH THE GTP ANALOGUE, GMPPNP.

Summary for 1F5N

• Entry DOI: 10.2210/pdb1f5n/pdb
• Related: 1DG3
• Descriptor: INTERFERON-INDUCED GUANYLATE-BINDING PROTEIN 1, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• Functional Keywords: gbp, gtp hydrolysis, gdp, gmp, interferon induced, dynamin related, large gtpase family. gmppnp, gppnhp., signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P32455
• Total number of polymer chains: 1
• Total formula weight: 68550.09

Authors

Prakash, B.,Renault, L.,Praefcke, G.J.K.,Herrmann, C.,Wittinghofer, A. (deposition date: 2000-06-15, release date: 2000-09-27, Last modification date: 2023-08-09)

Primary citation

Prakash, B.,Renault, L.,Praefcke, G.J.,Herrmann, C.,Wittinghofer, A.
Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism.
EMBO J., 19:4555-4564, 2000

PubMed Abstract: The interferon-gamma-induced guanylate-binding protein 1 (GBP1) belongs to a special class of large GTP- binding proteins of 60-100 kDa with unique characteristics. Here we present the structure of human GBP1 in complex with the non-hydrolysable GTP analogue GppNHp. Basic features of guanine nucleotide binding, such as the P-loop orientation and the Mg(2+) co-ordination, are analogous to those of Ras-related and heterotrimeric GTP-binding proteins. However, the glycosidic bond and thus the orientation of the guanine base and its interaction with the protein are very different. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein cannot approach. This has consequences for the GTPase mechanism of hGBP1 and possibly of other large GTP-binding proteins.

PubMed: 10970849
DOI: 10.1093/emboj/19.17.4555

Experimental method

X-RAY DIFFRACTION (1.7 Å)