1f5n

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spinqualitylabelsall models 1f5n, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1F5N is a Single protein structure of sequence from Homo sapiens with MG and GNP as ligands. Full crystallographic information is available from OCA.

Reference

Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism., Prakash B, Renault L, Praefcke GJ, Herrmann C, Wittinghofer A, EMBO J. 2000 Sep 1;19(17):4555-64. PMID:10970849

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